Steve Jobs At Stanford Commencement

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
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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

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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 overallleadership 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.

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 ... Show more content on Helpwriting.net ...
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

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 Оі–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 ОІ/Оі–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

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 aDNA
.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 ... Show more content on Helpwriting.net ...
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 specificamino 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

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+

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 modifyenzyme
structure ... Show more content on Helpwriting.net ...
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

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
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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 вЂђSH 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

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 Helpwriting.net ...
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

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 Г… (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 Оі 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

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

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

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 ...
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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

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%

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 Helpwriting.net ...
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

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

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 theprimary 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.

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

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
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"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 inThe 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.

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
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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

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 О±–Helixes and ОІ–sheets. The
a–Helixes form the backbone of the protein and help during the folding process. The ОІ–sheets can form in parallel and antiparallel pleated sheets.
When the О±–helix or ОІ–sheet is formed, the total volume available to the translational ... Show more content on Helpwriting.net ...
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

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

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 givenprotein 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

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, ... Show more content on Helpwriting.net ...
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,

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 descriptionPressure (psi)Damage description
Steel frame–metal building1.25
1.50
2.50
5.00Metal 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 system1.00
1.25
1.50
3.00Partial collapse of walls that have no fenestrations
Walls and roof partially collapse

Complete collapse
Steel or concrete frame with unreinforced masonry or infill cladding1.00
1.50
2.00
2.50
5.00Failure of incident wall face
Walls pushed in
Roof slab collapse
Complete frame collapse
Reinforced concrete or masonry shear all building 4.00
6.00
12.0Roof and wall deflect under loading. Internal walls damaged
Building has major

Pbgd Polypeptide Chain Analysis
The PBGD polypeptide chain consists of 313 amino acids and is approximately 57 x 43 x 32 Г… in size. Crystal structure of PBGD revealed a highly
flexible protein with three equally sized О±/ОІ 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 content on Helpwriting.net ...
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 В± 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 65oВ¬В¬В¬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 onprotein stability. The
Gln204 residue is on the surface of the central domain and located away from

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

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 sideВchain 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 Helpwriting.net ...
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

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

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 thesecondary 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

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

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

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 Helpwriting.net ...
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,

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
5вЂІ–UTR of human vascular endothelial growth factor (hVEGF) encompasses IRES elements.

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 Helpwriting.net ...
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,

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

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 Helpwriting.net ...
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

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 Helpwriting.net ...
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

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

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