kimkiki236

kimkiki236

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Harvard University

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Project Management1English3Biology9

1.Functional groups can modify the properties of organic molecules. In the table below, please indicate whether each functional group is polar or nonpolar and hydrophobic or hydrophilic. Which of these functional groups are found in proteins and lipids? You may use the text or any other resource.

Functional

Polar or

Hydrophobic or

Found in all

Found in many

group

nonpolar?

hydrophilic?

proteins?

proteins?

–OH

–CH2

–COOH

–NH2

–SH

–PO4

Polypeptides and proteins are made up of linear sequences of amino acids. In its functional form, each protein has a specific three-dimensional structure or shape. Interactions among the individual amino acids and their side chains play a major role in determining this shape.

a) How are amino acids linked together to form polypeptides or proteins? What is this type of bond called?

b. There is a group of proteins known as oncofetal antigens (ofa), what is their function?

c. Define the four structures ofa protein.

d. What kinds of bonds hold each of these together?

Primary:

Secondary:

Tertiary:

Quaternary:

e. Describe how the structures above might change if denatured by high heat or by a chemical that can denature protein.

 3. Use your understanding of the proteins in living organisms to predict the outcome of the following experiment. Be sure to explain your reasoning.

Experiment: A globular protein that is ordinarily found in aqueous solution has these amino acids in its primary structure: glutamic acid, lysine, leucine, and tryptophan. Predict where you would find each amino acid: in the interior portion of the protein (away from water) or on the outside of the protein (facing water). (Hint-Figure 3.10 of the textbook is a good reference.)

Many proteins are enzymes (they catalyze reactions). Thus, it is necessary to review how reactions take place. Reduced organic compounds tend to contain stored energy in C–H bonds. As a general rule, the greater the number of C–H bonds, the greater the amount of potential energy stored in the molecule. Answer each question in the chart as it relates to the two reactions shown at the top. Be sure to be prepared to explain the reasoning behind your answers.

Reaction 1:

CH4 + 2O2 → 2H2O + CO2

(methane)

Reaction 2:

6 CO2 + 6 H2O → C6H12O6 + 6O2

a.
Is the reaction exergonic or endergonic?

b. Is the reaction spontaneous?

c. Is the reaction anabolic or catabolic?

d. Is ∆G (the change in free energy) positive or negative?


5. All metabolic reactions in living organisms are enzyme mediated. Each enzyme is specific for one (or only a very few similar types of) reaction. Given this, there are approximately as many different kinds of enzymes as there are reactions.

a. What characteristics do all enzymes share?

b. What characteristics can differ among enzymes?

6.How can enzyme function be mediated or modified? To answer, complete columns a and b below.

a. What factors can modify enzyme function?

b. What effect(s) can each of these factors have on enzyme function?

c. What role(s) can modification of enzyme function play in the cell?

Answer: ask google

Respond to the following in the form of a short essay. Your essay should consist of at least five paragraphs.

Charles Dickens’s Hard Times is a novel divided into three books. These books are titled “Sowing,” “Reaping,” and “Garnering.” Explain how each book’s title relates to the events, characters, and themes that Dickens addresses in it, and analyze how the novel’s three sections convey Dickens’s central message about rationality and logic in mid-nineteenth-century England.

Cite specific examples from the novel in your response. Use the notes you take in the Reading Guide and the questions you answer in both the Reading Guide and the Student Guide to help you formulate your response.

You will hand in your completed response on the final day of this unit.

Process

You should always use a process for your writing that includes planning and drafting. To complete this assignment, you will do the following:

• Review the assignment instructions and grading criteria thoroughly. The writing assignment you complete in this unit will be graded against a rubric that assesses the essay in a number of categories. These categories focus both on the essay’s contents and its clarity.

o Read the rubric on the last page of this document. Keep the criteria listed on the rubric in mind as you complete the writing assignment.

o Remember to write in standard formal English and use the third person (no personal opinions) and the present tense.

• Complete a plan for your essay.

• Begin drafting your paper, using your plan as a guide.

• Review and revise your first draft. You should try to have another person read your work and give you feedback as part of your revision process.

• Write the final draft of your project. Be sure to follow these requirements and recommendations when completing your draft:

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BACKGROUND

The amino acid sequence for a protein that is associated with the onset of Huntington's Disease in humans is 582 amino acids long and is provided below. This disease is autosomal dominant and results in a prolonged degeneration of nerve cells in the brain.

INSTRUCTIONS

1. For this assignment, use any method you determine most feasible (i.e. programming in MATlab, R script, Crystal Ball, Witchcraft/Hocus Pocus, etc.) to decipher the amino acid composition of this protein and answer the 15 questions associated with this protein and its associated amino acid structure.

2. You will be calculating proportions (percentages - %) for this assignment. Calculate all proportions to 1 decimal place and make sure you have rounded up or down correctly. If unsure, use a spreadsheet program such as Excel to display your proportional calculations to 1 decimal place.

3. Spelling matters (Incorrect spelling will be graded as such - incorrect).

5. Download/copy the sequence and review the questions so you can double check your numbers before proceeding through the homework.

Huntington Disease Associated Protein Amino Acid Sequence

The first amino acid below ('m') represents the amino (NH3) terminus of this protein. The last amino acid in this sequence represents the carboxy (COOH) terminus and is the very last 'c' at the bottom of this protein sequence structure. The amino acids are numbered individually across the rows (left to right) beginning from the amino terminus (#1) to the carboxy terminus (#582).

mvskreniat

hhlyqawdpv

pslspattga

lisheklllq

inperelgsm

syklgqvsih

svwlgnsitp

lreeewdeee

eeeadapaps

spptspvnsr

khragvdihs

csqfllelys

rwilpsssar

rtpailisev

vrsllvvsdl

fternqfelm

yvtltelrrv

hpsedeilaq

ylvpatckaa

avlgmdkava

epvsrllest

lrsshlpsrv

galhgilyvl

ecdllddtak

qlipvisdyl

lsnlkgiahc

vnihsqqhvl

vmcatafyli

enypldvgpe

fsasiiqmcg

vmlsgseest

psiiyhcalr

glerlllseq

lsrldaeslv

klsvdrvnvh

sphramaalg

lmltcmytgk

ekvspgrtsd

pnpaapdses

vivamervsv

lfdrirkgfp

cearvvaril

pqflddffpp

qdimnkvige

flsnqqpypq

fmatvvykvf

qtlhstgqss

mvrdwvmlsl

snftqrapva

matwslscff

vsastspwva

ailphvisrm

gkleqvdvnl

fclvatdfyr

hqieeeldrr

afqsvlevva

apgspyhrll

tclrnvhkvt

tc

CARBOXY TERMINUS

I posted this before with no replies! It's urgent.

I need this decoded because I don't have any access to any coding methods in order to answer the following questions:

a.) a.) What is the name of the least abundant amino acid in this protein?

b.) What proportion of the total amino acids in the protein does this individual amino acid represent?

c.) What is the proportion of essential amino acids included in this protein sequence?

d.)The amino acid sequence from residues 73-85 is represented by the amino acids EEEWDEEEEEEAD, how would you generally classify this small region of the protein? Choose from: neutral, hydrophilic, hydrophobic, negatively charged, positively charged

e.)Two amino acids are present in the same proportion in this protein, which two are those?

f.)Which class of amino acids is the most abundant in this protein?

g.) What amino acid(s) is/are present at locations 572 and 582 in the Huntington Disease protein (Full Amino Acid Name(s)).

h.)What type of structure could form between these amino acids that could help stabilize this protein's structure?

i.) Which class of amino acids is least abundant in this protein?

j.)Summed together, how many hydrophilic amino acid residues are present in this protein?

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