Exam 6: Proteins: Secondary, Tertiary, and Quaternary Structure

A major stabilizing factor in the triple helix is a ____ structure such that ____ residues from the three strands stack along the center of the triple helix.

Alpha helices are stabilized primarily by:

Discuss the structure of fibroin proteins.​

Amino acid sequence is:

Describe β-turns in peptide chains.​

Antiparallel β-sheets have:

A Ramachandran plot shows:

In the tertiary structure of a protein, a hydrophobic interaction could form between the R-groups of which two amino acids?

If the following section of a polypeptide is folded into an α-helix, to which amino acid is the carbonyl group of alanine hydrogen bonded? Ala-ser-val-asp-glu-leu-gly

Which of the following does not contribute to the spontaneous nature of the protein folding process?

The outward face of a(n) ____ consists mainly of polar and charged residues, whereas the inner face contains mostly nonpolar, hydrophobic residues.

Flexible, disordered segments of proteins are commonly high in the amino acid:

Collagen has the following characteristics EXCEPT:

In the majority of α-helixes, each peptide carbonyl is hydrogen bonded to the peptide N−H group ____ residues farther ____ the chain.

A β-barrel would most likely be composed of ____.

Planarity of the peptide bond means that no rotation occurs about the _____ bond while rotation is allowed about the ____ and ____ bonds.

Enumerate the characteristics of the α-helix structure of proteins.​

All are true about the tertiary structure of the enzyme triose phosphate isomerase EXCEPT: