Tertiary Proteins Structure Forces

Tertiary Proteins Globular
. The 3–D tertiary structure of polypeptide proteins globular and is the result of interactions that
occur between R groups. Tertiary structure is a result of the bonds between sidechains of amino
acids, the R groups. The structure and bonds involve alpha helices, beta pleated sheets, and also
regions unique to each protein. Tertiary proteins are held together by four different types of forces;
hydrogen bonds, hydrophobic interactions (including Van der Waals interactions), ionic bonding
(electrostatic interactions), and disulfide bridges (strong covalent bonds). Hydrogen bonds occur
within and between polypeptide chains and the aqueous environment. Hydrogen bonding forms
between a highly electronegative oxygen atom or a nitrogen atom and a hydrogen atom attached to
another oxygen atom or a nitrogen atom. This links the amino acid ... Show more content on
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PrPc (a healthy prion) generally functions in this way but when unhealthy PrPSc comes into contact
with healthy PrPc it converts healthy to unhealthy. This disrupts the cell and the cell will make
another healthy PrPc in its place. This is how the disease unfolds. The cell replaces the healthy
protein that has become unhealthy PrPSc; only for it to then be converted to unhealthy. PrPSc
eventually converts all healthy PrPc proteins to PrPSc. PrPSc; the misfolded and unhealthy prion
acts as its own chaperone. Proteosomes exist to destroy proteins that misfold. Our defense
mechanisms do not recognize the PrPSc as foreign and therefore do not destroy it. It continues to
proliferate as it turns PrPc to PrPSc. Since PrPSc is hydrophobic it tends to hide from water and turn
inward and clump together in the cells. This is called aggregation. Eventually the PrPSc overtakes
and kills the cell and leave the appearance of tissues looking spongy. New cells do not grow in dead
cells place and PrPSc finds new cells to invade as the disease progresses (Cobb & Surewicz,
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History Of Opitz Syndrome : A Disease Characterized By A...
Opitz syndrome is a disease characterized by a defect along the ventral midline of the human body.
Some of these abnormalities include a cleft lip, heart defects, wide–spaced eyes (hypertelerism),
laryngeal cleft, agenesis of the corpus callosum, and hypospadias. An important irregularity in
patients is the effect disrupted proteins have on the corpus colloseum. The corpus colloseum is a
neuronal component that separates the two halves of the brain. This protein is imperative because it
controls MID–1 or the midline. The MID–1 protein also forms homodimers, which associate with
microtubules in the cytoplasm, especially during fetal development. Therefore, MID–1 is involved
in formation of multiprotein structures, acting as anchor points to ... Show more content on
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I found this topic interesting and informative because it defined the multiple ways that a protein
could be affected in the body and lead to a disease. While some people find biochemistry as a whole
intimidating, I find it fascinating that pathways and complexes can interconnect and link.
Interconnections can cause more than one result. This concept helped me understand how a disease,
such as Opitz syndrome, is so challenging to cure. Curing the effects of B–box 1 or 2 may or may
not lead to realignment of microtubules. There could be downstream effects that take place in other
areas. As a result, hard work and a plethora of experimentation is necessary to be able to isolate
pathways and cure this troubling disease.
Question 2: (29 pts) In the article, "Effect of an Ala81His Mutation on the Met80 Loop Dynamics of
Iso–1–cytochrome c," figure 1 includes a portion of the protein sequence.
a. (5 pts) What is the difference between using the terms, identity and homology, when comparing
protein sequences.
In terms of comparing protein sequences, "identity" means that the protein sequences have identical
amino acids in their sequence. The percent of identical amino acids indicates the percent of
"identity" between amino acids.
In terms of comparing protein sequences, "homologous" means similarity between protein
sequences. The proteins may be even more homologous because of similar – but not identical –
residues. Often, homology is

Examination Of Biliverdin Ix Beta Reductase
Examination of Biliverdin IX–Beta Reductase
October 10 2014
Joel Langford It is evident that there are many significant biological syntheses that take place in this
world. This includes the synthesis of bilirubin (BR) from biliverdin (BV) with biliverdin IX–beta
reductase (BVR). BV is one of three products produced from heme being catalyzed by heme
oxygenase. Now, BVR, as seen in Figure 1, is known as an enzyme that catalyzes the reduction of
BV's double bond to a single bond on the second and third pyrrole ring. In other words, BVR
reduces BV, which is hydrophilic, using NADPH and yields the product bilirubin, which is
hydrophobic (1). The schematic for this mechanism is shown below...
Schematic 1: It is important to note ... Show more content on Helpwriting.net ...
This paper will examine the three–dimensional structure of BVR and its specific interactions.
Among the 204 amino acid residues in BVR, its secondary structure contains alpha–helices, beta–
sheets, and turns, as seen in Figure 2 (4). The arrangement of these helices and sheets represents that
of a Rossmann Fold (5). The protein structure of a Rossmann Fold contains six parallel beta strands
that are linked to two pairs of alpha helices (6). In BVR, there are ten beta–sheets, six of which lie
parallel forming the Rossmann Fold, and there are seven alpha–helices which seem to be
"wrapping" around the Rossmann Fold, which explains the beta–alpha–beta–alpha–beta topological
order. For example, this includes the central beta–sheet and the two groups of alpha–helices. While
it may seem rather easy to comprehend, it seems important to make note of the simple interactions
or facts relating to the coenzyme nicotinamide adenine dinucleotide phosphate, NADPH, and the
substrate mesobiliverdin, MBV, which is a tetrapyrrole compound. To start, this reaction is a
reduction reaction in which the MBV is the compound being reduced. The NADPH, carrying
hydrogens, is the reducing agent, also meaning it is oxidized by the MBV (the NADPH simplified
interactions with the protein and amino acids can be noted in Figure 3. Now, on a side note, looking
closely at Figure 4 and then comparing the MBV (which is mesobiliverdin IV–alpha) to heme, one
can note that they look extremely

Structures of Proteins Essay
Proteins are polymeric chains that are built from monomers called amino acids. All structural and
functional properties of proteins derive from the chemical properties of the polypeptide chain. There
are four levels of protein structural organization: primary, secondary, tertiary, and quaternary.
Primary structure is defined as the linear sequence of amino acids in a polypeptide chain. The
secondary structure refers to certain regular geometric figures of the chain. Tertiary structure results
from long–range contacts within the chain. The quaternary structure is the organization of protein
subunits, or two or more independent polypeptide chains. The primary structure of a protein is
simply the sequence of amino acids. The structure or ... Show more content on Helpwriting.net ...
There may also be sections where the secondary structure is neither helix nor sheet. Then the
structure is called a random structure, indicating that it folds in random directions. The amino acids
in an alpha helix are arranged in a right–handed helical structure resembling a spring. The alpha
helix is the most common form of regular secondary structure in proteins. The beta–sheet is the
second form of regular secondary structure in proteins consisting of beta strands connected laterally
by three or more hydrogen bonds, forming a generally twisted, pleated sheet. The beta–sheet is
sometimes called the beta pleated sheet since sequential neighboring atoms are alternately above
and below the plane of the sheet giving a pleated appearance. Turns are the third of the three
"classical" secondary structures that serve to reverse the direction of the polypeptide chain. They are
located primarily on the protein surface and accordingly contain polar and charged residues.
However, they are not very common in discussions of protein structure today.
The tertiary structure of a protein molecule, or of a subunit of a protein molecule, is the arrangement
of all its atoms in space, without regard to its relationship with neighboring molecules or subunits.
Tertiary structure is simply the grouping of different separate secondary structures, such as multiple
helices or multiple sheets or a combination of helices and sheets.
The final structure of the protein is the quaternary

The Dysfunction Of Bureaucracy : A Review On Party City Inc.
The Dysfunction of Bureaucracy: A Review on Party City Inc.
Bureaucracy is defined as "a large group of people who are involved in running a government or
system of authority but who are not elected" (Merriam–Webster). Society and business, as a whole,
are run by bureaucracies. Individual businesses are not elected are not run like a republic. They are
run by powerful individuals who do what is best for the company and for themselves. The summer
after my sophomore year of high school, I had the opportunity to work at a company run by a
bureaucracy. This company is known as Party City. Many people do not see this company as a
towering giant of a company overwhelming the competition with its every increasing wealth;
however, it is ... Show more content on Helpwriting.net ...
On my first day I met my managers, Dakota and Stephanie, and my general manager Amber. I was
also allowed to meet on my very first day, the sectional and regional managers. Each position gave
more money but also increases their responsibility. With this clear cut system, no one questioned the
leadership, and everyone knew who was in charge. Positions were also identified with color of
shirts. Party members wore gray t shirts, party leaders wore black polos, assistant managers wore
red, and general managers wore blue polos. With this simple identification it was easy to identify
anyone on the job in order to complete tasks as efficiently as possible.
In bureaucracy, there also is a clear and distinct division of labor that is noticeable to almost anyone.
At party city I was in charge of the cash register during my shift and stocking the solids, and making
balloon orders over the phone. This was just one of the many jobs. There were back dock workers
that would unpack from the shipments, there were costume organizers, and party staff. Every
employee had a specific team and each team had a team leader and the team leaders had a manager.
This points to the fact that the work is divided into the structures of authority. The division of labor
is intertwined with the hierarchical structure of authority. With this simple division of the tasks and
labor required to make the company run, the workers are

Muscle Research Paper
There are three different types of muscle; skeletal, cardiac and smooth.
Skeletal muscle consists of long cylindrical cells which, under a microscope, appear to be striated
with bands throughout length of the cell. The nuclei of the multinucleated cells, located along the
plasma membrane, lie along the periphery of the cell, thus forming swellings which are visible
through the sarcolemma. The plasma membrane of the muscle cell, also known as sarcolemma, is
densely invaginated by transverse tubules that saturate the cell. The cytoplasm, or sarcoplasm of the
muscle cell, contains a calcium– storing sarcoplasmic reticulum, which is the specialised
endoplasmic reticulum of a muscle cell. For the vast totality of the volume, the cell is filled with

Hydrogen Bonding Answers
Questions:
1. What type(s) of bonding is (are) involved at each of the following levels of protein structure
(4pts.):
a. Primary– Joined by peptide bonds at this level. Peptide bonds are a type of covalent bond between
two different amino acids where the carbonyl group on one amino acid bonds with the amino group
on the other amino acid thus releasing water (H2O).
b. Secondary– Hydrogen bonding is involved at the secondary level of protein structure. Hydrogen
bonding occurs at regular intervals along the polypeptide backbone. Hydrogen bonding is an
intermolecular force much weaker than covalent or ionic bonds that occurs between a hydrogen
atom bonding to fluorine, nitrogen or an oxygen atom.
c. Tertiary– Tertiary structure is formed between the bonding of the R–groups connected to the
polypeptide backbone. The types of bonding that occur between the R–groups are hydrogen
bonding, ionic bonds, and covalent bonds. A common covalent bond that occurs at the tertiary level
is disulfide bridges between R–groups. Hydrophobic interactions also occur at the tertiary level.
d. Quaternary– At the quaternary level bonding occurs between separate polypeptide chains using
hydrogen bonding, ionic bonding, and covalent bonding.
2. The case study background focuses on a specific sulfhydryl ... Show more content on
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Then a neutralizer breaks the disulfide bonds to uncurl the hair. Disulfide bonds are covalent bonds
formed between two thiol–containing r–groups. This is done using a neutralizer, commonly
hydrogen peroxide via the process of oxidation. Oxidation is the process of loosing electrons. The
new hair formation is formed using reduction. Reduction is the changing of the state of oxidation
specifically the gaining of electrons. This gain allows the cysteine residues for form a new shape by
creating new disulfide bonds. This is the process of hair chemically changing from one shape to

Week 6 Enzyme Research Paper
HW#6 Enzyme Essay
It can be seen that enzymes are basically proteins with large molecules.. An enzyme is made up of
long natural chains of amino acids linked together by peptide bonds, so it chemically contains
carbon, hydrogen, oxygen, nitrogen, and some sulfur. The proteins are tertiary in which they fold up
to give the enzyme its active site. The initial level of the enzyme involves the sequence of amino
acids. Every amino acid has an amino group, a carboxyl group, a hydrogen group, and an R group
that can be different with each amino cell all connecting to the alpha carbon. Based on what the R
group is, it can be determined whether or not an amino acid can be uncharged, polar, a base, an acid,
or charged. The secondary level then involves

Why Is Protein Denaturation
Protein Denaturation–an Important Concept in Biology!
Biology has many topics which unfold the truths of nature in an interesting way. Protein
denaturation is one such topic which shows how denaturation of protein is found in common
household activities like cooking.
What are proteins?
Proteins are found in all living beings. They are large molecules which are composed of folded
amino acid chains. Every protein has its unique shape and functions based on its shape. Proteins are
like keys that fit into certain shaped locks around the body. Proteins are required for speeding up
biological processes, recognizing antibodies, providing substances, regulating physiological
processes, regulating genes, transporting substances and responding to signals ... Show more content
on Helpwriting.net ...
Incorporation of air bubbles and absorption of protein molecules to the air– liquid interface also
cause denaturation of proteins. The extent of change in conformation of proteins is based on the
flexibility of the proteins. Highly flexible proteins denature more readily than the rigid ones do at
the air– liquid interface. College Biology courses have many more exciting topics that show up a
treasure of ideas and knowledge for students who are interested in the subject. Some of them may be
intriguing and as such students need expert help from online Biology tutors who make even the
challenges in the subject easy to understand with their custom made solutions and approaches.
Biology assignments at college level are vast demanding time and research which may not be within
the reach of many students. College biology assignment help is a succor for such students from
tutors whose expertise in the subject allows them to produce assignments which are original and
plagiarism free with well researched

Is Tachylectin 5a A Protein Found During The Immune System...
Tachylectin–5A is a protein found in the immune system of the Japanese horseshoe crab, Tachypleus
tridentatus. Tachylectin–5A, which has a PBD reference number of 1JC9, is mainly found in the
hemolymph plasma of horseshoe crabs (1). This protein was determined on June 8th, 2001 via x–ray
diffraction (1). The X–ray diffraction results in an absorbance of 2.01 Å (2). It shows that the protein
contains 269 residues, and the molecular weight ot is 380–400 kDa (2). Proteins similar to
tachylectin–5A have been found in various organisms like slime molds, sponges, bony fish, and
lancelets (3). Tachylectin–5A is structurally related to the fibrinogen γ fragment, which is found in
mammals' plasma; and it is similar to a protein in humans called ficolin, which is involved in host
defense through nonself–recognition (4).
Tachylectin–5A is an ellipsoidal molecule that is an asymmetrical monomer, which is subdivided
into three different domains that interact with each other (2). The primary structure of Tachylectin–
5A constitutes 269 amino acid residues (1). The amino acid composition of this protein has a cis–
peptide bone between Arg–218 and Cys–219 (3). It contains one protein modification called
prryolidone carboxylic acid, which is the twenty–fourth amino acid in the sequence (1). And the
secondary structure of the protein consists of 16% alpha helical and 24% beta sheets. There are 9
helices with 44 amino acid residues and 19 beta sheets with 66 residues involved in total (1). The

What Are The Four Levels Of Protein Structure
. Amino acids have attributes that make them hydrophilic or hydrophobic. Amino acids that contain
electrically side chains are able to connect or attract with water molecules. Amino acids that contain
partial charges or polar side chains, forming hydrogen bonds, are hydrophilic or attract with water
molecules. Amino acids with nonpolar side chains are hydrophobic or do not attract with water
molecules.
2.
2. 3. The four levels of protein structure are primary, secondary, tertiary, and quaternary. All of the
levels are made from the primary structure of the protein. Primary structure contains covalent bonds
and is the foundation and basis for the other levels of a protein. Secondary structure is a repeated
continuation of a peptide chain.

NLRPCHT Case Study
NLRPNACHT 3D models showed a typical structural fold and conserved ATP–binding motifs
Domain analysis revealed that all the NLRP proteins (excluding NLRP10) comprised of three
functional domains; N–terminal PYD, central NACHT and variable numbers of C–terminal LRRs.
NLRP1 has two additional domains, FIIND and CARD towards the C–terminal region (next to
LRR), whereas NLRP10 lacks the LRR (Fig. 1a; Supplementary Table. S1). Consistent with recently
resolved structures [mNlrc4 (4KXF) and OcNOD2 (5IRL)], and sequence analysis results, we
outlined three functional sub–domains of NACHT/NOD modules; (a) the nucleotide–binding
domain (NDB) positioned after Pyrin domain (PYD), (b) the helical domain 1 (HD1) and (c) the
winged helix domain (WHD) ... Show more content on Helpwriting.net ...
S3) were considered for further studies (Fig. S1a). A close visual inspection of docked
conformations showed a conserved ATP–binding pattern except for NLRP5, NLRP8, and NLRP9.
Till date, only two ADP–bound NLR structures have been resolved experimentally [mNlrc4 (4KXF)
and OcNOD2 (5IRN)] and both the structures shared a common nucleotide–binding orientation28,
29. Therefore, we adopted the manual approach of docking; where the γ–phosphate group of ATP
was deeply buried inside the cavity, and adenine moiety was positioned outward (Fig. S1b). To
understand the binding mode and dynamic stability of ATP, MD simulations of both the prepared
ATP–bound NLRPNACHT complexes [complex I (AutoDock) and complex II (manually docked)]
were performed for 60ns time scale. Manually docked NLRPNACHT–ATP complexes exhibited a
good binding stability The experimental evidence suggested that Walker A (GxxxxGK[S/T]) of
AAA+ ATPase proteins has the major contribution in nucleotide binding and particularly, it
coordinates the β/γ–phosphate group of NTPs28–37. To acquire a stable NLRPNACHT–ATP
complex for interaction analysis, a combined root mean square deviation (RMSD) of Walker A and
ATP was calculated, and the result indicated a stable array of deviation in manually–docked systems
except in NLRP13 (Fig. 2a). Further, we analyzed the total numbers of intermolecular H–bonds
between ATP and NLRPNACHT from the obtained trajectories as the function of

Functional State Of Secondary Structures Essay
Functionally similar proteins (i.e. Orthologous protein BLOCKs) evolve to create amino acid
divergence at locus specific positions (Gaucher, Miyamoto and Benner, 2001; Wang and Gu, 2001).
Different BLOCKs evolve at a different rate. However, for a given family (or BLOCK) it is constant
(Dickerson 1971; Dayhoff and Schwartz, 1978). The divergence, although alters primary sequences,
sequence of secondary structure largely remains unaltered, the one that acts as a determinant for
functional state of proteins of homologous family (Shen, Jones and Mohrenweiser, 1998). The fact
that not all hetero–pairs (total 190) contribute equally to the evolution of a BLOCK (Figure 2, A1
and A2), characterizing their differential role in relation to its properties is of central importance.
Further, it remains a challenge to understand the acquired substitutions at the primary sequence level
and the maintenance of secondary structures for functional state. Present study is an attempt to gain
insight into the mechanism of substitutions based on observed hetero–pairs and positional diversity
in relation to protein's structure and function.
3.1. Observed homo and hetero pairs are sensitive parameters in the study of evolution
Henikoff and Henikoff (1992) pioneered the concept of BLOCK and developed BLOSUM series of
fundamental matrices that utilize observed hetero–pairs for computation of odd–scores. These
matrices (e.g. BLOSUM62) got wide application in Bioinformatics studies []. When identical

Design And Hermeneutic Phenomenology Research Paradigm Has...
10.4.5 Critique
The critique of this model derives principally from the criticisms that can be levelled at the research
methodology, particularly its non positivist approach, although a rationale for the single case study
design and hermeneutic phenomenology research paradigm has been made above (Ch 5,6).
Within its own epistemological terms a legitimate criticism of such a model of management might
derive more generally from its potential irrefutability, following Popper's criticism of the
"pseudosciences" , where a counter example is re–interpreted within the frame of the model so as
not to contradict it, for example a non charismatic leader's behaviour might be reinterpreted as
having elements of the charismatic process, although they not being obvious.
A second critique might be made building on the assumption that managerial effectiveness within an
organisation in predicated on their ability to lead, mobilise and direct subordinates. As a result, it
might be argued that the model covers a very small element of the overall leadership and
management process, focussing exclusively on the manager's activity and leadership with their own
subordinate team, and missing the larger organisational function of the leader, their entrepreneurial
activity, and engagement with supraordinate managers. This is an acknowledged failing, based upon
Parson's collectivist notion of power (@@@@ above), and there are some speculations and
proposals for further research noted below.

Protecting Against Terrorist Attacks in Urban...
Introduction
Blast protection, until recently, has only needed to be considered when constructing underground
shelters and military bunkers. Currently, however, there is a need for urban buildings and similar
structures used consistently by the general public to withstand forces from nearby explosions. This
need is due to the recent climb in terrorist attacks in urban or crowded environments. These attacks
have used the lack of blast resistance in these buildings as a means for creating widespread havoc
through detonating an improvised explosive device (IED). These devices range from explosives
planted inside a structure to roadside or vehicular bombs. An urban environment causes even
relatively small explosions to be extremely potent ... Show more content on Helpwriting.net ...
Structures that collapse in an urban environment result in casualties inside the building and also
result in collateral damage that may cause nearby structures to also collapse. This effect was seen in
the collapse of the World Trade Center in New York City, although this collapse was not a result of
the initial explosion. Had the towers not collapsed, it is estimated that close to half of the deaths
could have been prevented (Dwyer). It is therefore vitally important for buildings that suffer damage
from explosions to remain structurally stable for as long as
Building description Pressure (psi) Damage description
Steel frame–metal building 1.25
1.50
2.50
5.00 Metal siding anchorage failure
Sheeting torn off and internal walls damaged. Danger from falling objects
Building stands, but cladding and internal walls destroyed as frames distort
Building completely destroyed
Unreinforced masonry bearing wall system 1.00
1.25
1.50
3.00 Partial collapse of walls that have no fenestrations
Walls and roof partially collapse
Complete collapse
Steel or concrete frame with unreinforced masonry or infill cladding 1.00
1.50

2.00
2.50
5.00 Failure of incident wall face
Walls pushed in
Roof slab collapse
Complete frame collapse
Reinforced concrete or masonry shear all building 4.00
6.00
12.0 Roof and wall deflect under loading. Internal walls damaged
Building has major

Protein Butterfly Journey
My Journey to Become A Protein Butterfly
By: Courtney Hofer
Hello, my name is Kelly the protein. I am going to tell you my story how I came to be a beautiful
protein butterfly. There are two different process of becoming a protein butterfly;they are translation
and transcription.
Has I was going to say the first one is translation. Translation is where I made a twin mRNA
molecule in the nucleus of an eukaryotic from a DNA.There were four adventures I went on during
translation. My adventures begins in the RNA enzyme combining the DNA and aparting the two
nucleotide chain. After I went through that adventure, one nucleotide chain of the DNA works as a
form for fixing them together into the mRNA. My third journey through this process was when ...
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Transcription is where I translate the list of nitrogenous bases in the mRNA at the cell's ribosomes. I
want to tell you what a codon is and tell you my five other journeys. A codon is where each three
nitrogenous bases in an mRNA that helps a specific amino acid added to me the protein butterfly.
My adventure begins when a ribosome comes together to an mRNA in the cell's cytoplasm. Then on
my journey my BFF codon goes throught the ribosome, tRNA shares with the amino acid to the
ribosome. My other friend anticolon does a great job of putting three nitrogenous bases in tRNA to
help the codon in mRNA. My third adventure was where tRNA bring a type of amino acid; then she
breaks the code in the mRNA into a guide of amino acids. Following is my second to last adventure
was when my friend ribosome and rRNA makes the amino acid together. My last adventure was the
funnest because this is the part where I turned into a protein butterfly. :) Here is how the ending
goes: My other friend protein chain goes raises til the ribosome gets a end codon on the rRNA. After
that ribosome leaves equally mRNA and me the protein

Hierarchy Of Needs: A Case Study
Authority The authority of the Missouri state agencies is one, which is based on a machine
bureaucracy. The four main departments each operates under a director, with some having even
divisions underneath the departments. This is a classic machine bureaucracy in whom "members of
the strategic apex make the big decisions; managers and standardized procedures govern day–today
operations" (Bolman & Deal, 2013, pg. 77).
Coordination
In the Missouri state agencies handling child services, there were instances of both vertical and
horizontal coordination, but not all were operated effectively. The vertical coordination of the
departments administering children services primarily composed of authority and rules and policies.
There was some instances of lateral coordination through meetings and task forces, but not enough
to offset some of the structural conflicts. A focus on decentralizing some of the coordination would
provide the creativity needed to launch new ideas. The four departments of the Missouri state
agencies, DSS, DESE, DMH, and DH, all relied on an authority of the director to implement
initiatives and ensuring the actions aligned with the goals of the organization. The rules and policies
of the departments were in place to "limit individual discretion and help ... Show more content on
Helpwriting.net ...
120). For Gary Strangler, his struggles with not meeting his personal needs stemmed from reaching
the top of the hierarchy at self–actualization. Strangler felt discouraged due to his inability to bring
together all the Missouri state agencies under a comprehensive plan to improve the welfare of
children in the state of Missouri and make services more efficient. The pilot programs of Families
First, Family Preservation Services, and Caring Communities were not enough to create across the
board

The Bioinformatics / Molecular Evolution Lab
The purpose of the Bioinformatics/Molecular Evolution lab is to explore a particular protein given
to us by its amino acid sequence. By entering this protein into the Entrez Protein Database in the
National Center for Biotechnology Information, and using tools within this database such as Jpred,
SMART, and Protoparm, the given protein could be fully analyzed. This experiment was very
successful as our particular protein could be identified, and the tools within the NCBI database
allowed us to fully analyze both chemical and physical aspects of this protein.
Bioinformatics combines both aspects of biology and key components of computer science. When it
comes to DNA, the smaller molecules that make up DNA, along with the sequence of these ... Show
more content on Helpwriting.net ...
In addition, it has many cofactor binding sites such as Mg and Zn and interacts non–covalently with
metal ions.5
This particular protein of interest is made up of 524 amino acids. When further analyzing this
protein, the Jpred results displayed in Figure 2 give a further understanding of the secondary
structure of this protein. It is apparent that the secondary structure of alkaline phosphatase, tissue
non–specific isozyme isoform 1–precursor contains primarily alpha helices, yet also contains a few
beta sheets. The figure displays the alpha helices by long, red tube like figures and the beta sheets as
green arrows. Because this figure contains many more long red tubes than green arrows, it is
apparent that the secondary structure contains mostly alpha helices. What results in the secondary
structure of a protein is the regular pattern of hydrogen bonding between the N–H from the peptide
and the C=O groups of the amino acids. These two structures that result in the hydrogen bonding are
found relatively close to one another within the linear sequence. Within this regular pattern of
hydrogen bonding is where the alpha helices and beta sheets are found. What primarily makes up the
secondary structure of our studied protein, alkaline phosphatase, tissue non–specific isozyme
isoform 1–precursor, are alpha helices. Alpha helices are rod–like structures that are stabilized as a
result of the hydrogen bonds between the N–H and the C=O groups found among the main

Digital Fabrications Architectural And Material Techniques
ARC 5205 Advanced Theory
Professor Neil Leach
STUDENT NAME: Deborah Wintringer Ariosa
BOOK TITLE: Digital Fabrications Architectural and Material Techniques
DATE: 11/03/2016 PAGES READ: 60–87
The book presents the methods behind digital fabrication in a very clear way, the method this
chapter is focused on is folding. For most people "folding" seems pretty obvious, it is a term often
used in design studios and architectural projects and could be considered a design principle. This
chapter gives us the full range of what folding stands for, how it can be used and shows clear
examples depending in the material employed. The chapter is mostly focused on the material
operation of the folds and only slightly mentions the theoretical concept and formal tactic of folds.
When one adjusts digital designs to work with physical forms a different type of ingenuity is
possible, materials can take shapes and forms never thought conceivable. Folding used in
architecture has helped produce a variety of fascinating work that has indisputably molded
contemporary design. It can turn flat surfaces into a three–dimensional one and create structure with
geometry. Folding materials is therefore effective at numerous scales.
A great advantage of folding is how it creates structural stiffness with geometry. When we add folds
onto a planar material, it gains toughness and rigidity. Strategically placed folds enable the material
to potentially span longer distances, the folds also often turn the

Ovalbumin Research Paper
Ovalbumin is the main protein that is found in egg whites, which make up 55% of the total protein.
Its main function is to provide a reserve of amino acids for developing embryos. [1] Proteins are
purified by the method of sulphat e precipitation. This technique is useful as it removes large
amounts of contaminant proteins.
Some proteins are made up of amino acids that contain sulphur. There are only two amino acids that
contain sulphur, Methionine and Cysteine. Methionine has a thioether side chain, –(CH2)2–S–CH3,
whereas, cysteine has a thiol group side chain, –CH2–SH. In proteins, the cysteine side chains form
covalent bonds between each other to produce disulphide bonds, as a result of oxidation. The
process of oxidation produces stable ... Show more content on Helpwriting.net ...
It reacts with free sulfhydryl groups to yield a mixed disulphide and TNB (2–nitro–5–thiobenzoic
acid). DTNB targets the conjugate base (R–S) of free sulfhydryl groups. TNB is a bright yellow
coloured species that is produced in the reaction and has a high molar extinction coefficient which
can be seen in the visible range. [3]
The molar extinction coefficient, originally reported by Ellman (1959) [4], was 13.6 x 106M–1cm–1
at 412nm and pH 8.0. [5] The increase in absorbance at 412nm can be used to measure reactive thiol
groups. The colour change observed is due to the presence of S– anions. DTNB is very useful as a
sulfhydryl assay reagent because of its specificity for ‐SH groups at neutral pH, high molar
extinction coefficient and short reaction time. [6] Thionitrobenzoate is produced by a further
reaction which takes place in the presence of excess thiol, RSH.
SDS (sodium dodecyl sulphate) is a chemical agent that is used to denature protein molecules by
straightening the polypeptide chain. Disulphide bonds are found in the tertiary structure of proteins
and would not react if the protein remained folded. Without SDS, there would not be any thiol
groups

Alzheimer's Report: Layers In A Protein
Alzheimer's Report
Layers in a Protein
Primary folding is the first and most basic layer. This layer contains the sequence of amino acids
themselves. The structure and order of the amino acids is important because it helps determine the
interaction type seen in the protein while it is folding. The interaction of the amino acids will show
what the secondary and tertiary structure of the protein will be.
Secondary folding is the second layer. This folding includes structures that extend into one
dimension. It also includes α–Helixes and β–sheets. The a–Helixes form the backbone of the protein
and help during the folding process. The β–sheets can form in parallel and antiparallel pleated
sheets. When the α–helix or β–sheet is formed, the total volume available to the translational ...
This folding describes the arrangement of the amino acids. The shape of the acids is held in place by
the hydrogen bonds. A hydrogen bond is a dipole–dipole interaction between a hydrogen atom and
an electronegative atom. The hydrogen bonds are important because if they didn't hold the structure
of the amino acids in place, there would be no backbone for the protein.
Tertiary Folding includes hydrogen bonds as well as disulfide bridges. Hydrogen bonds can form
between side–chain groups. As with the disulfide bridges, these hydrogen bonds bring together two
parts of a chain that are a distance away from each other in terms of sequence. These bonds are
important because they help to form and stabilize the overall 3D structure of the protein.
Quaternary Folding contains hydrogen bonds, disulfide bridges, and salt bridges. Salt bridges are
ionic interactions between positive and negatively charged parts of amino acid side chains. These
bonds are all important in the fact that the subunits in this folding can interact with each other and
begin to form a larger protein. They help stabilize the final shape of the protein.
Intermolecular

Human Carbonic Anhydrase II ( Hca II )
Human Carbonic anhydrase II
Carbonic anhydrase (CA, EC 4.2.1.1) has around 16 isozymes, which are different isoforms, and
these have assorted tissue position 's subcellular and distribution, which are exist in plants, animal,
archaea, and eubacteria. However, not all of them are involved decisive physiological processes but
only some of them. For example, acid–base balance, respiration, biosynthetic reactions, and
electrolytes secretion are crucial physiological processes, which are affected by some of carbonic
anhydrase isozymes. The most significant feature of carbonic anhydrase is diffusion–controlled
metalloenzymes, which converts reversibly carbon dioxide to bicarbonate and proton.
This proposal focuses on human carbonic anhydrase II (HCA II), this enzyme has a tertiary structure
and 29 kD polypeptide, which is the most common isozyme and the fastest. The active site of this
enzyme (HCA II) includes a metal ion such as zinic ion, which is a tetrahedral by coordinating a
three histidine residues (His119, His96, and His94) and hydroxide ion the forth ligand (H2O263).
The most important function of HCA II is the mechanism of conversion carbon dioxide to
bicarbonate. This mechanism occurs by three steps:
His64–E–Zn–OH– + CO2 = His64–E–Zn–HCO3– + H2O = His64–E–Zn–H2O + HCO3– (a)
His64–E–Zn–H2O + H2O = H3O+–His64–E–Zn–OH– (b)
H3O+–His64–E–Zn–OH– = His64–E–Zn–OH– + H3O+

Complex Macromolecules: A Protein Study
Proteins are complex macromolecules which are essential for life of all organisms. They are
manufactured through the processes of transcription and translation, which take place inside the
cells. More specifically, they are synthesised by ribosomes (Shakhnovich, 2007). Figure 1.1 shows
the overall processes that can occur in making a fully functionally active protein. (Ghelis, 2012).
Functional properties of certain proteins include, but is not limited to: structural composition of the
cytoskeleton in cells, catalysing biochemical reactions and hormones such as insulin to regulate
blood sugar concentration (O'Connor & Adams, 2014). Proteins must therefore have a specific 3–
dimentional shape to allow them to carry out these functions. If their ... Show more content on
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Alzheimer's disease (AD) is the most common aging disorder affecting millions of people
worldwide (Apostolova & Cummings, 2007) and is caused by the misfolding of proteins, causing
neuronal degeneration (Ramirez–Alvarado, Kelly & Dobson, 2010). Structures known as sinile
plaques, which have inner cores of beta amyloid fibrils, are found in the brains parenchyma and on
the walls of the cerebral blood vessels of people with AD (Vinters, Wang & Secor, 1996). It was
discovered by John Hardy and his research team in 1991 that a hereditary form of Alzheimer's is
caused by a mutation in the amyloid precursor protein (APP) (Taubes, 1996) This protein is a
glycoprotein thought to carry out functions in neuronal survival and synaptic stability (Apostolova
& Cummings, 2007). When mutated, the alpha helix native structure is transformed into a beta sheet
conformation. This results in the insoluble protein accumulating in the brain and extracellular
aggregation of beta amyloid (Forloni et al., 2002), by catalysing other proteins into their abnormal
state – an infective conformation (Ashraf et al, 2014) and aggregate, which is when continued
negative feedback will occur with the generation of more insoluble fibrils (Apostolova &
Cummings,

Enzymes: The Four Levels Of Protein
1. Enzymes are a type of protein. There is four levels of structure in an enzyme. The first level of
their structure is called the primary level, and in this level, there is a sequence of amino acids. The
way these amino acids are determined is an "R" group, based on this "R" group, an amino acid can
vary, such as uncharged, polar and uncharged, basic, as well as acidic. The second group of their
structure is called the secondary group, and this group involves the bonding of hydrogen in the
amino and carboxyl backbones. The third, or tertiary stage involves various types of bonding
between "R" groups of the Amino Acids. The final Quarternary level occurs with two or more
polypeptide chains. In enzymes, the factors that modify enzyme structure ... Show more content on
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The four types of organic molecules are carbohydrates, lipids, protein and nucleic acids. A
carbohydrate's monomer is a monosaccharide, and its functions are to provide energy. An example
of a carbohydrate is glucose. A lipid's monomer is glycerol and its functions are to keep storage of
energy and to form cell membranes. An example of a lipid is milk. A protein's monomer is an amino
acid, and some of its functions are to create blood cells, and regulate enzymes. A nucleic acid is
made up of nucleotides, and some examples of them are DNA and RNA. A nucleic acid's function is
to make genetics, which are the basic building blocks of all living things.
6. The function of starch is to convert into glucose for energy, it is used by animals. The function of
glycogen is as an energy storage in animals. Cellulose, the most abundant organic compound on
earth is a component of cell walls in plants. Chitin is a component of exoskeletons and cell walls of
plants.
7. Low–density lipoproteins Are known as the "bad cholesterol" while High–density lipoproteins are
known as the "good cholesterol". Because cholesterol can't dissolve in blood, too much "bad
cholesterol" with its thick and hard deposits can clog arteries. However having "good cholesterol"
can help get rid of

Scarlet Letter Analysic- Form, Plot, Tone, Essay
Scarlet Letter Analysis
Form, Structure and Plot: The structure that Hawthorne puts the Scarlet Letter is very tight, and is in
essentially three parts, each revolving around the scaffold. The first scaffold scene, Hester confesses
her sin of adultery to the crowd in the light of day. The second scaffold scene takes place in the
middle of the book at night; it is the climax of the plot. Dimmesdale climbs onto the scaffold, and
asks for Hester and Pearl to join him. This is not a confession, as there are no witnesses, except for
Chillington. The third scaffold scene is at the end of the novel. Here, Dimmesdale is on the scaffold,
with Hester and Pearl. It is light out, and they are speaking to a crowd. Here, Dimmesdale confesses
his sin. ... Show more content on Helpwriting.net ...
"His face darkened with some powerful emotion, which, nevertheless, he instantaneously controlled
by an effort of his will, that, save at a singly moment, its expression might have passed for
calmness." The majority of the sentence is secondary structure. There are two primary– "his face
darkened" and "he controlled." The primary structure allows us to understand what is happening at
the moment, while the secondary allows us to see an image of what Hawthorne was trying to get
across– cynicism. With the first part of the sentence– "his face darkened with some powerful
emotion", he can imagine his expression growing into a scowl, the air around him darkening as he
meets eyes with Hester.
Tone: The tone in The Scarlet Letter is moralizing, impassioned, formal, and skeptical. The narrator
of the story pretends to be unbiased, although it is blatantly obvious he does not think highly of
Puritans. He often spends one to two paragraphs discussing the problems he has with Puritan
society, or a law that had effect at the time.
Bibliography
Hawthorne, Nathaniel. The Scarlet letter. New York: Barnes & Noble Children's Classics, 2001.
Print.
"SparkNotes: The Scarlet Letter: Context." SparkNotes: Today's Most Popular Study Guides. N.p.,
n.d. Web. 3 Oct. 2011. .
"The Scarlet Letter Hypocrisy Quotes." Shmoop: Homework Help, Teacher Resources, Test Prep.
N.p., n.d. Web. 3 Oct. 2011.

Secondary Structure Prediction
When analyzing the secondary structure predictions of the query sequence from the five prediction
programs, the majority of the programs seemed to detect the presence of one long, uninterrupted
helix on the N–terminal side of the pilE protein. However, some programs, such as PORTER
(Pollastri et al., 2005) and SSpro (Magnan et al., 2014) indicated the presence of two helices
interrupted by a small gap of random coils. While these results appear to contradict each other at
first, upon further inspection, this can be explained by the fact that when two helices are very close
to each other, some algorithms may erroneously pick it up as 1 long helix since secondary prediction
programs are not 100% accurate. Thus, in the consensus secondary ... Show more content on
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One possible reason for this discrepancy that while these species represent species that are homologs
of each other, some of their secondary structures may slightly differ from one another. Another
possible reason for this discrepancy may be because, as briefly mentioned before, secondary
structure prediction programs are not always accurate and thus, there could have been an error made
in one of the programs, allowing for detection of an extra beta strand or for a beta strand to go
undetected. This is perfectly illustrated by the PORTER server, which mysteriously predicts a helix
spanning amino acid residues 104–113 of the query sequence when all the other programs predicted
either a beta strand or random coil in that range instead (Figure 1b). Since PORTER was the only
program to predict a helix in this range, it is considered an outlier and thus, it can largely be ignored
as an error when making the consensus secondary structure prediction. The initial domain
architecture was generated based on the known pilE protein in Neisseria gonorrhoeae (control
sequence) and consisted of two domains, the N–terminal domain and the pilA domain. Using the
metaserver InterPro, the N–terminal domain was predicted to span amino acid residues 2–29, while
the pilA domain was predicted to span residues 36–161 (Finn et al., 2017). Although there seemed to
be a somewhat high correspondence between the secondary structure prediction analysis and the
domain architecture

What Is Organisational Behaviour
Organisational behaviour investigates the impact that individuals, groups and structures have on
behaviour within organisations, as this knowledge can optimise the effectiveness of these
organisations. A way to understand organisational behaviour is to understand the organisational
psychology behind it (Murray, Poole, & Jones, 2006). Organisational psychology is the branch of
psychology that is dedicated to the study of individual psychological phenomena within
organisations and ways in which organisational processes has an influence on people. The field of
organisational behaviour was developed primarily by the contributions of psychology, sociology and
anthropology. Each of which has contributed significant ideas for organisational developments
(Stuit, Szirbik, & De Snoo, 2007). They pooled in a separate field known as organisational
behavioural. Three other disciplines exerted less influence in the development of organisational
behaviour which is economy, science policies, and history. The relationship ... Show more content
on Helpwriting.net ...
Robbins, et.al, (2013) states "It is a field of study that investigates the impact of individuals, groups
and structures on behaviour within organisations, in order to apply the knowledge gained in
improving the effectiveness of an organisation". Murray, Poole, & Jones, (2006) believes that
organisational behaviour is "the study and application of knowledge on how people act within
organisations. It is therefore a human tool for the benefit of people and applies generally to the
behaviour of people throughout class organisation". The main aim is to have an organisational
behaviour pattern that allows improving the organisations adapted to people who are different,
because the human side is the decisive influence in the possibility of achieving the achievements of
the establishment, being undoubtedly that the study of change is one of the most important aspects
in all organisational

The Guiding Elements Of Holocracy
The guiding elements of holocracy include a range of ways to reorganise the governance structure of
organisations. This section will look through these elements through two lenses. First, we'll use
Zappos as an example to explain the elements. But secondly, we'll also explain how these structures
differ from the traditional model for organisations.
Roles not job descriptions
Perhaps the striking difference between traditional governance structures and the holocracy model is
evident in job descriptions. Whilst we are typically used to job titles such as the vice president,
manager and so forth, holocratic systems remove these altogether. For example, as we cited John
Bunch above, we didn't list any specific role for him at Zappos because ... Show more content on
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Circle structure
Traditional organisations are generally structured around a hierarchic model. You have someone
above you in the organisation until you get to the top. But holocracy removes this hierarchical
structure in favour of a democratic circle structure.
What this means is that the roles form a circle structure within the organisation. For example, certain
roles regarding the organisation's finances might form a larger circle. However, there is hierarchical
organisation in the way the circles are laid out. Certain circles are 'above' others in terms of
management. Nonetheless, each circle has the ability to self–organise.
The authority to decide the roles, to assign tasks and to take responsibility lies within the circle, not
a single person or a different part of the organisation.
Hsieh explained this structure is "about moving faster, being more responsive and adaptable, and
enabling employees' talents and passions to shine". Each circle can gather around and adjust the
roles and tasks ahead without having to run it through a hierarchical system.
Rapid iterations replace big re–organisations
Another element that comes together with this untraditional structure is the way holocracy deals
with re–organisation. Unlike in traditional organisations, where updates to structure happen every
few years, under holocracy the structure is updated in rapid iterations.

The aim is to keep the organisation up–to–date

Rna Review : The Rna
RNA GQ structures in cap–independent translation initiation.
RNA G–quadruplex (GQ) is a secondary structure that can act as both necessary elements of
translation and as translation repressors.1–3 The role of GQ structures in translational modulation
depends on the context in which the GQ structure is present.4 However, it is well established that
these structures mostly inhibit translation.2,5–7 In fact, rational introduction of GQ structures
specifically downregulate the expression of targeted genes.8,9 AlternativelyHowever, the presence
of the GQ structures in IRES reverses its inhibitory role. In the cases of FGF and VEGF where the
GQ structures are present in the context of an IRES, they act as essential elements for translation
initiation.10,11 HoweverNevertheless, the mechanism by which the GQ structures play a context–
dependent regulatory role is unknown. Here we report that the direct interaction of the
independently folding GQ domain with the 40S ribosomal subunit (40S subunit) is critical for the
cap–independent translation initiation in a cellular IRES. It is a unique example of a non–canonical
and well–defined RNA secondary structure that has the ability to recruit the 40S subunit directly and
modulate the function of a cellular IRES.
The IRES mediated translation initiation, although initially observed in viral mRNAs, has also been
identified in many cellular mRNAs.12 The 5′–UTR of human vascular endothelial growth factor
(hVEGF) encompasses IRES elements.

The Discovery Of The Network Devices
1. Describe the steps you would take to determine the needs of the organization (the discovery of the
network devices)
As a consultant that was brought in to determine the needs of the organization, the primary starting
point is content discovery. The art of content discovery is to get an understanding of the business, its
network structure, organizational requirements and the resources that are available. Because the
number one rule in all problem solving manifests, is first to know and get an understand the
problem, the problem that you are tasked with or trying to solve.
Therefore, the first element of content discovery is to get an understanding of the organization. Who
is the company, what industry do they operate in, what services or products do they provide, what is
their mission statement, what are their daily operations, are many of the questions that needs to be
answered, often times before the job starts. The second element is to understand the organization
from an internal point of view. It starts with understanding the structure of the organization, getting
a high–level organization chart to help determine the divisional structure of the organization, their
communication methods, the Service Level Agreements that they have in place, and their
geographical profile in order to know whether there are additional sites in other regions. The next
step within the second element is to get the structure and technical level of local and remote IT
divisions, their

A Matrix Structure : An Organization
A matrix structure will not be successful if an organization's employees are not trained with the
ability and skills necessary to operate within the structure. Employees must have the right mindset
and behaviors in order to operate in an environment that is constantly conflicted with multiple
bosses and simultaneously pursuing multiple aims (Bartlett and Ghoshal, 1990; Ford and Randolph,
1992). The employees need to have the same goals within the organization so there is less
competition among them. For example take two teams one is in marketing and one is in
development if both of them have different goals to achieve this leads to conflict among both teams
creating a dysfunctional workplace. These same employees also need to know exactly what their job
requires them to do. The matrix structure adds flexibility to the organization but the company needs
to make sure that the responsibilities of the top executives are not the only known responsibilities,
those job indicators need to be exchanged between all levels of the workforce. The flexibility the
structure provides can lead to untimely decisions. This is created by the fact that the matrix structure
requires input and collaboration among its staff. The employees may have trouble deciding whose'
input is needed because the interpersonal skills of the employees is lacking leading to untimely
decisions that could result in a loss of quality. Or the employees may just become divisionally
focused and not see the organization

Tertiary Structure
Task 2
a) The tertiary structure refers to the structural arrangement of amino acids that are found far away
from one another along the polypeptide chain. The tertiary structure is overall a three dimensional
shape of a protein molecule. It will bend and twist to achieve maximum stability. The shape of a
tertiary structure is made when the secondary structure folds in on itself and is held in place by
many bonds and interactions formed by the R groups in the amino acid chain. The bonds and
interactions involved are hydrogen bonds, ionic bonds, hydrophobic interactions and disulphide
bonds. These bonds and interactions are located in different areas of the tertiary structure, the
hydrogen bonds are located inbetween polar R groups, ionic bonds are located between charged R
groups, hydrophobic interactions are located between nonpolar R groups and disulphide bonds are
formed generally in the endoplasmic reticulum by oxidation ."Hydrogen bonds may form between
different side
chain groups." Hydrophobic interactions are brought about in an aqueous site. The
tertiary structure is held together mainly by interactions that are located at the R groups.
A protein with a tertiary structure could be a myoglobin protein. The myoglobin protein has a alpha
helix. Bonds between the side groups of the amino acid are responsible for holding together the
tertiary structure of myoglobin. The myoglobin is found in the ... Show more content on
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It has an alpha helix and a tertiary structure for each subunit. The same forces and bonds that create
tertiary structure also hold subunits together to form the complete protein for the quaternary
structure. An example of a protein that has a quaternary structure is Hemoglobin. Hemoglobin is
created by four peptide chains that have formed a working protein. It has more than 2 peptide chains
and creates a protein, thus making it a quaternary structure
Task

SIP: Self-Inhibitory Peptides
4 SIP: Self–inhibitory peptide design
SIP's inputs are the protein fasta sequence and the PDB file.
We have the sequences and the PDB files for all proteins that have been successfully aligned with
active peptides. We design self–inhibitory peptides targeting these proteins using SIP. The process
consists in four steps that will be briefly described here: The first step is the secondary structure
prediction followed by the second step, which is the disorder prediction. These first two steps are
based on the protein sequence only. The third step is the selection of segments of 20 amino acid
long, with low disorder and helical secondary structure, within the protein. And finally, the fourth
step is the calculation of the the energy score based of the structural information from the PDB file.
A good candidate self–inhibitory peptide must have a stable secondary structure.
To be realistically considered as good candidate self–inhibitory peptides, they should be as stable as
possible. That's why SIP selects segments of the target protein that are 20 amino–acid long with
helical secondary structure and low disorder probability.
A good candidate self–inhibitory peptide must have a strong interaction energy with the protein
target. ... Show more content on Helpwriting.net ...
It is the most important criteria to determine if the segment is a good potential self–inhibitory
peptide or not. The lower the energy score, the stronger the interaction is likely to be between the
self–inhibitory peptide and the protein target. To discriminate a good self–inhibitory peptide from a
weak one, we set a threshold value of –40 for the energy score. Segments with an energy score
below this threshold are considered as good candidate self–inhibitory

Pbgd Polypeptide Chain Analysis
The PBGD polypeptide chain consists of 313 amino acids and is approximately 57 x 43 x 32 Å in
size. Crystal structure of PBGD revealed a highly flexible protein with three equally sized α/β
domains. The N terminal domain (domain 1) and the central domain (domain 2) have similar
structures, both being doubly wound parallel beta sheets. Domain 3 (C terminal) is an open faced,
anti–parallel, three stranded beta sheet with one side covered in 3 alpha helices, this domain
interacts with both 1 and 2. In domains 1 and 2, each sheet has 4 parallel and 1 anti parallel strand
with alpha helical segments packed against each face and are orientated parallel to one another.
Domains 1 & 2 are motifs and they are both related by a two–fold axis. Domain ... Show more
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PBGD is the third enzyme in the biosynthetic pathway of heme production and when the production
of this enzyme is stopped, or in some cases the activity of the enzyme is hindered, this disease may
develop. Acute Intermittent Porphyria causes abdominal pain, neurological and psychiatric issues
such as hallucinations and also results in an increase in levels of ALA heme precursors and PBG in
urine. The p.Gln204Lys mutation in exon 10 is evidenced to directly link to the development of AIP.
Analysing enzyme activity with the wild form of the mutation shows the relationship between
mutant and AIP. Glu204Lys showed to have 46 ± 0.72% of wild–type activity, which did not
correlate with the expected 50% decrease in enzyme activity when associated with mutants so,
further analysis was undergone. Heat inactivation studies showed that the PBGD is very stable but
the wild enzyme lost 30% of its activity post incubation at 65o¬¬¬C for 240 mins. This data relates
to the large number of ion pairs, which are built into the enzyme structure. The half life of the
mutant affected enzyme was three times less than the wild enzyme type at 100 minutes which relates
to AIP as a decrease in enzyme activity can lead to symptoms of AIP. This then evidences that the
Gln204lys has a negative effect on protein stability. The Gln204 residue is on the surface of the
central domain and located away from

Two Major Components Of Lactate Dehydrogenase In Biology
Lactate dehydrogenase is an enzyme that is found in most living organisms which catalyzes the
conversion of lactate to pyruvic acid. It converts NAD+ to NADH and back again. Pyruvate is
converted to lactate when oxygen isn't present and the reverse reaction takes place (Wikipedia).
There are two major subunits of lactate dehydrogenase which are the M form and the H form. The
M form, major subunit in muscles, is efficient in the conversion of pyruvate to lactate. The H form,
major subunit in the heart, is efficient in the conversion of lactate to pyruvate. Despite the
differences in structure of the M and H form, there's enough similarity for hybrids of the M and H
form to form (Goodsell).
The oxidization of lactate requires the binding of NAD+ to the enzyme first before lactate. A
hydride ion is rapidly transferred in either direction yielding a mixture of the two teranary
complexes, enzyme–NAD+–lactate and enzyme–NADH–pyruvate. The dissociation of pyruvate
from the enzyme followed by NADH takes place. The rate of dissociation of NADH is the rate
limiting step. This remains valid in the reverse reaction as the binding of NADH takes place first
and then the substrate, pyruvate, is able to bind (Busby). The reverse reaction of pyruvate to lactate
is the thermodynamically favored reaction. When oxygen is insufficient, it's purpose is to restore
NAD+ to allow glycolysis to continue without stopping (Aalto). Although this reaction has a Gibbs
Free energy value is –200kJ/mol, 93%

Power, Authority, And Authority
Power and authority organize people in bureaucratic structures. The hierarchical structure of these
organizations dictates the scope of authority that each individual has relative to their respective
position. Standardized rules, methods, and procedures within the bureaucratic structure stimulate
strict discipline as an essential element for success. The organizations are impersonal places to work
and do not conform to the needs of the workers. Historically, power and authority in bureaucratic
structures has limited individual personal decision–making, restricted individual opportunities for
creativity, denied individual opportunity to develop a sense of self and restricted the potential for
diversity in the workplace in public administration.
Power and authority are different concepts; however, the terms function reciprocally in the
bureaucratic structure of an organization. The organization's power is centered at the top and the
authority flows from the top down through ordered levels of management: from senior executives to
regional managers to departmental managers and supervisors who work with the frontline
employees. Authority and control from different levels of hierarchy within a bureaucratic structure
are defining to the entire purpose of the organization. All departments have organizational charts,
and everyone understands who is in charge and their responsibilities. Job descriptions are detailed
and specialized and management monitors outcomes, which in turn

Steve Jobs At Stanford Commencement
Anjal Lamsal
Professor Mary Hidalgo
English 101 v2
22 October 2017
"2005 Stanford Commencement" – Steve Jobs
According to the speech of Steve Jobs at Stanford Commencement, he presents his opinion and
history as evidence. He makes himself to be a person who carries on even in the darkest of times and
who has overcome many obstacles when things didn't look good. The speech begins with his
statement of dropping out of college in front of students graduating from the good university. The
speech made bigger impacts in the student's life. Steve jobs has used many types of dialogue in the
speech to give the importance of the education. His words in this speech has enlightened the young
blood to ... Show more content on Helpwriting.net ...
He promotes with his speech structure. He uses simple structure to make his speech super powerful
just like drops of water makes the ocean. As he uses the rule of three to make his speech even better.
s there is a beginning, middle and end in the life of the mythic hero. The three stories Jobs tells in
his speech are about connecting the dots (how he learned how every action/event in life is
connected), love and loss (how he found love and lost things/people close to him), and death (where
Jobs discusses his own battle with cancer and the fear of dying). In his first short story to the
audience, Jobs' does a successful job with his rhetorical method. He repeats the phrase "connecting
the dots" during the speech. He mentions that people can only connect those dots of life looking
backwards which gives a powerful meaning to the audience. Not only with the starting but he ends
his first story by telling that "you should trust in something to connect dots and make future better.
His timing and pace makes his speech so comfortable to the listeners that every word is familiar to
the audience and clear in meaning.
However, the second story lets the audience to truly measure their success. He brings pathos from
the audience in two separate ways. First, he explains about the trouble with his Macintosh. How he
got fired form the apple. Which made audience more attractive towards listening to the speech. He
connects his speech towards emotions by telling stories of his wife.
Jobs

Liver Catalase Lab Report
Effects of Temperature on Decomposition of H2O2 by Liver Catalase
Introduction A countless number of chemical reactions occur in the human body at any given time in
order to carry out cellular processes necessary for continued functioning. These reactions can
sometimes result in harmful byproducts such as hydrogen peroxide or H2O2. Catalase is an enzyme
contained within organelles called peroxisomes that decompose the toxic H2O2 down into water and
oxygen gas. Enzymes are a type of protein that are catalysts of biochemical reactions, meaning that
they speed up the rate of reaction through various ways by lowering the amount of activation energy
required for each reaction. Each enzyme has an optimal temperature range at which it functions ...
Catalase is found in nearly all aerobic organisms, and one molecule can break down millions of
H2O2 molecules every second. It works by first reducing a H2O2 molecule bonded to its active site
through taking an oxygen away with its Fe3+ component, which releases a water molecule into the
cytosol. Then, the enzyme will bond with a second H2O2 molecule and oxidize it by giving it the
oxygen from the first H2O2 molecule, releasing O2 and another water molecule into the cytoplasm.
This catalytic cycle then repeats indefinitely.
The purpose of this study is to test how changing the temperature of the liver, which was the
catalase source, would affect the rate of reaction with H2O2. If temperature increases then there
would be less O2 released because proteins denature when temperatures are too high, losing their
shape and ability to carry out their intended function.
Materials and Methods
For a detailed list of required materials, refer to the enzyme lab handout section C. The independent
variable in this study was temperature. The dependent variable was rate of reaction, measured
qualitatively on a scale of one to five based on the number of bubbles observed as the reaction took
place. The amount of liver and H2O2, the ambient temperature, and the observation time allotted for
each reaction were control variables that were kept constant throughout.
First, three small pieces of liver were placed into separate test tubes and covered with a small

Protein In Sports
Proteins are organic and complex compounds made of several amino acids that are linked and cross–
linked by the chains of peptide; hydrogen, van der Waals and the sulfhydryl forces respectively.
Among the biologically active compounds, proteins are made of varied chemical compounds.
Proteins can be grouped as simple proteins, conjugated proteins, and the derived proteins
(Rodriguez, 2009). Simple proteins yield amino acids and fewer carbohydrates when hydrolyzed.
Examples of these proteins include albuminoids, histones, albumins, glutelins, histones, globulins,
and protamines. Conjugated proteins are the simpler proteins that are combined to non–protein
compounds in the body. They include lecithoproteins, glycoproteins, nucleoproteins, hemoglobin, ...
Branched chain amino acids helps in maintaining the flow of the protein to the muscles. This will
help in reducing the loss of the muscles during the training and improve the synthesis of protein.
Branched chain amino acids helps in the sparing of the muscles as well as recovery after strenuous
exercise.
Importance of protein anabolism and catabolism in muscle building activities Anabolism is the
successive chemical reactions that synthesize smaller molecules into larger compounds through the
energy absorption. Catabolism is the chemical breakdown of complex molecules to smaller
molecules through the release of energy (Ramsey, 2002). The growth of the muscle depends on the
continuous balance of catabolism and anabolism. The synthesis of the muscles is made possible
through production of cortisol, a catabolic hormone from endocrine system. The process of
catabolism assist in the provision of energy required for the exercises that helps in the building of
the body (Ramsey,

Tertiary Proteins Structure Forces

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