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Local folding that occurs through hydrogen bonding between the amino group of one atom and the carboxyl group of another atom within the same polypeptide is known as:

A

Option A: secondary structure.

B

Option B: primary structure.

C

Option C: tertiary structure.

D

Option D: quaternary structure.

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Elin Hessel
Elin HesselLv2
28 Sep 2019

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Related questions

Each of the following can cause a protein to denature except:

Select one:

a. enzyme treatment

b. heat

c. change in pH

d. detergents

What factors can influence the speed of a reaction by an enzyme?

Select one:

a. The weakening of bond energies in the reactants

b. The closeness of the reactants to each other in the active site

c. The orientation of the reactants

d. All of these

A protein that is comprised of two or more protein chains that interact to make the overall structure is called the:

Select one:

a. quaternary structure

b. secondary structure

c. primary structure

d. tertiary structure

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

Select one:

a. Dipole-dipole

b. Hydrogen bonding between the carbonyl group and amino group

c. Salt bridges

d. Peptide bonds

A molecule that is similar in terms of the correct structure to the substrate for an enzyme will probably be a:

Select one:

a. competitive inhibitor

b. regulator

c. cofactor

d. noncompetitive inhibitor

Tertiary proteins are determined by the primary amino acid sequence. Should a protein, in which the order of all amino acids is reversed have the same tertiary structure?

a. Yes even though the amino acid sequence is reversed the tertiary folding remains the same

b. yes the protein remains the same

c. yes and no it depends if the amino acid is palindromic

d. no the amino acid sequence is the same but the amino and carboxyl termini are not

1. The level of protein structure that is stabilized primarilyby non-covalent interactions between the side chains within asingle polypeptide chain is refered to as its:

A) primary structure

B) secondary structure

C) tertiary structure

D) quaternary structure

E) none of the above

2. Collagen, a strong fibrous protein found in connectivetissue, bone, and the extracellular matrix, has a structure inwhich three left-handed helices wind around each other to form aright-handed triple helix. The primary structure of collagen has arepeat unit of -(Gly-X-Pro)- Which of the following bonds stabilizethe collagen triple helix? (mark all that apply)

A) Hydrogen bonds between hydroxyproline residues

B) Hydrogen bonds between N-H and C=O

C) Ionic bonds between amino acid side chains

D) Hydrogen bonds between charged amino acids

3. The non-covalent forces that stabilize the Beta-strandconformation of peptides include:

A) H-bonds between amide C=O and amide NH

B) Van der Waals packing between the peptide backbone atoms

C) Van der Waals packing due to side chain interdigitation

D) Only A and B above

E) None of the above

4. What is the approximate length difference of a 22-kDasingle-stranded ?-helical protein segment vs. a 22-kDasingle-stranded ?-strand protein segment? Assume a mean residuemass of 110 Da. Show work.


5. Circular dichroism measurements have shown that the peptidebackbone of poly-l-lysine (KKKKKKK) adopts a random coilconformation at pH 7.0, but becomes ?-helical as the pH is raisedabove 10. This observation is known as the

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