BIO 1140 Study Guide - Midterm Guide: Electronegativity, Macromolecule, Intermediate Filament

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6 Apr 2018

School

University of Ottawa

Department

Biology

Course

BIO 1140

Professor

Caroline Petit- Turcotte

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Document Summary

The molecular structure provides clues as to how the molecule will react with its environment. Proteins need to function in areas that are hydrophilic (such as the cytoplasm) or hydrophobic (such as the membrane). You should be able to look at the structure of molecules and determine which areas contribute to its polarity and how it will affect its location and function. (4 marks) Tips: while you are not expected to memorize the structure of all 20 amino acids, you are expected to be able to analyze their structure. Pick a few, look at the radical groups and discuss how their electronegativity contributes to their polarity. Answer: microtubules and microfilaments: which fiber is the smallest in diameter? (choice of answers microfilaments, microtubules, intermediate filaments) Answer: microfilaments: which fiber protects the nucleus? (choice of answers microfilaments, microtubules, intermediate filaments) Answer: intermediate filaments: which fiber interacts with dynein? (choice of answers microfilaments, microtubules, intermediate filaments)

Related Questions

Protein Structure

a.Different function of proteins and examples:

b. Protein building blocks:

1. atomic composition of building block:

2. "parts" or "functional groups" of the building block:

c. Importance of side chain (R group):

d. Hydrophobic amino acids characteristics:

e. Hydrophilic amino acids characteristics:

f. Charged amino acids characteristics

Copy and complete the table below regarding the characteristics and which groups in the polypeptide interact together at each structural level of the protein.

	characteristics	groups interacting
Primary structure
Secondary structure
Tertiary structure
Quartenary structure

Value: 2

Choose the correct statement(s). You may choose more than one answer.

[mark all correct answers]
a. Proteins are the building blocks of amino acids.

b. Enzymes are a type of protein.

c. Quartenary structure consists of two or more polypeptide chains interacting.

d. Amino acids are made of carbon, hydrogen, nitrogen and phosphorus.

e. The primary structure of a protein is formed due to the interaction of side groups.

Value: 3

Put the following statements regarding the structural levels of a protein formation in the correct order.

Below is a sequence of events. Place them in the order they should occur, number 1 being the first item. Select the step number from the drop down next to each item.

Items to order:

1. Individual amino acids are bonded together via peptide bonds.

2. Two or more polypeptide chains interact via bonds.

3. Hydrogen bonds form between neighboring amino acids within a polypeptide chain allowing the chain to coil or form pleated sheets.

4. Side groups (R) of the individual amino acids interact with each other allowing the protein to assume its three dimensional shape.

Value:4

Put the following statements regarding the structural levels of a protein formation in the correct order

Individual amino acids are bonded together via peptide bonds.	1 2 3 4
Two or more polypeptide chains interact via bonds.	1 2 3 4
Hydrogen bonds form between neighboring amino acids within a polypeptide chain allowing the chain to coil or form pleated sheets.	1 2 3 4
Side groups (R) of the individual amino acids interact with each other allowing the protein to assume its three dimensional shape.	1 2 3 4

Value: 5

Hydrophobic amino acids will be found _______________.

a. In the interior (inner core) of a protein, away from the watery environment.

b. in the interior of a plasma membrane.

c. Both A and B

d. Neither

Value: 6

A protein's function is defined by ____________.

a. enzymatic reactions

b. it's shape.

c. chain of nucleotides.

d. the presence of carbon and hydrogen.

Value: 7

Which of the following is NOT considered a protein function?

a. transport of substances across membrane

b. enzymatic reactions

c. provides structural support

d. carries genetic information

1. A polypeptide chain has a large percentage of acidic and basic amino acids in it. The R groups of these amino acids form ionic interactions, which helps the protein to maintain itâs structure. This particular polypeptide works well under an optimum pH of 7. Ignoring effects of strong acids and bases on peptide bonds, what will happen to the tertiary structure of the protein if you move it stomach acid, which has a pH of 1-2. Why? Be specific regarding what influence the pH will have on the bonds maintaining tertiary structure in the molecule. Include the amino acid charges of the acidic and basic amino acids at the acidic pH, as well as the concept of pK in your answer. Assume that acidic amino acids have a pK of approximately 4.7 and basic amino acids have a pK of approximately 10.

2. Ignoring peptide length (or lack thereof) where would this portion of a polypeptide be most likely to be found: On the inside or on the outside surface of a protein floating around in the cytoplasm? Explain

3. A mutation occurs in the SRC kinase such that the tyrosine on the loop over the active site is changed to aspartic acid. This mutation mimics phosphorylation.
a. knowing what you know about the properties of phosphate groups and aspartic acid, why does aspartic acid mimic phosphorylation?
b. What would be the implication of this mutation on the function of the SRC kinase?

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?

BIO 1140 Study Guide - Midterm Guide: Electronegativity, Macromolecule, Intermediate Filament

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