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23 Nov 2019

7. Which of the following interactions are generally considered to be unfavorable?

a) Interaction between Lys and Glu at neutral pH, assuming standard pKa values of Lys and Glu.
b) Interaction between a backbone amino group and a side chain carbonyl group
c) Interaction between two alpha helices
d) Interaction between Arg and Lys side chains at a pH of 2, assuming standard pKa values for Arg and Lys.

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Bunny GreenfelderLv2
28 Feb 2019
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Related questions

The sequence of amino acids is considered to be the ________ structure of a protein.

Select one:

a. secondary

b. tertiary

c. quaternary

d. primary

The pattern the backbone folds, for example alpha-helix or beta pleated sheet, is the ________ structure of a protein.

Select one:

a. quaternary

b. secondary

c. tertiary

d. primary

Which type of forces stabilizes the primary structure of a protein?

Select one:

a. Salt bridges

b. Hydrogen bonding between the carbonyl group and amino group

c. Dipole-dipole

d. Peptide bonds

The interaction of the side chains on the amino acids, for example hydrophobic attractions, is the ________ structure of a protein.

Select one:

a. quaternary

b. secondary

c. tertiary

d. primary

1. The side chain of tyrosine is considered to be polar because even though it is reminiscent of phenylalanine it also has two types of atoms that have large differences in electronegativity with asymmetry at the terminus.

a.) True

b.) False

2. Which of these changes in primary structure will be certain to cause a loss of protein activity?

a.) Asp to Glu

b.) His to Lys

c.) Trp to Ser

d.) Gly to Pro

e.) Not enough information is given since any one of these changes could be severe depending on the context of the situation

3.The difference between fetal and adult hemoglobin with regard to oxygen binding occurs because fetal hemoglobin has an amino acid substitution in one of its chains that results in a histidine (adult version) being replaced by a serine (fetal version).

a.) True

b.) False

4. What will likely happen if the side chains of aspartate and histidine at pH 5 are next to each other in a polypeptide chain?

a.) The side chains of these amino acids will be uncharged and there will be no electrostatic effect.

b.) The side chains of these amino acids will be charged and they will attract each other.

c.) The side chains of these amino acids will be charged and they will repel each other.

d.) Not enough information is given to determine the effect.

5. A beta pleated sheet:

a.) can occur between two different polypeptide chains
b.) can be formed by either intramolecular or intermolecular hydrogen bonds
c.) can only form when cysteines form disulfide bridges within this structure
d.) forms when side chains of D and E attract each other
e.) both a and b

1.) Tertiary structure of proteins can be created by:

a)

Hydrogen bonding between atoms in the amino acid side chains.
b)

Hydrogen bonding between atoms in the peptide backbone.
c)

Electrostatic interactions between atoms in the peptide backbone.
d)

Hydrophobic interactions between atoms in the amino acid side chains.
e)

Both a and d are correct.

2.) SDS PAGE

Separates proteins based on charge.

Separates proteins based on size.

Separates proteins based on size and charge.

Separates proteins based on isolectric point.

More than one of the above.

3.) Which would be the best pH range to isolate a protein (pI = 6) from a cation exchange column whose resin has a pKa of 4?

pH's below 4

pH's above 6

pH's

4.) The peptide DRAMA has how many ionizable protons?

2

4

12

10

between 4 and 6

None of the above

All of the above (any pH)

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