BackInteractions of amino acids on the interior of proteins are key to the shapes of proteins. In group (a), which pairs of amino acids form hydrophobic interactions? In group (b), which pairs form ionic interactions? Which pairs in group (c) form hydrogen bonds?
a. 1 Pro . . . Phe
2 Lys . . . Ser
3 Thr . . . Leu
4 Ala . . . Gly
What kind of bond would you expect between the side chains of the following amino acids?
c. Aspartic acid and asparagine
What kind of bond would you expect between the side chains of the following amino acids?
b. Alanine and leucine
Is the bond formed between each pair in Problem 18.76 covalent or noncovalent?
For each amino acid listed, tell whether its influence on tertiary structure is largely through hydrophobic interactions, hydrogen bonding, formation of salt bridges, covalent bonding, or some combination of these effects.
a. Tyrosine
What type of R group interaction is the most likely between the alanine and isoleucine residues?
Oxytocin is a small peptide that is used to induce labor by causing contractions in uterine walls. It has the primary structure Cys-Tyr-Ile-Gln-Asn-Cys-Pro-Leu-Gln. This peptide is held in a cyclic configuration by a disulfide bridge. Draw a diagram of oxytocin, showing the disulfide bridge.
How do the following noncovalent interactions help to stabilize the tertiary and quaternary structure of a protein? Give an example of a pair of amino acids that could give rise to each interaction.
a. Hydrophobic interactions
Which of the following amino acid pairs are the most likely to form hydrogen bonds?
Which of the following amino acid pairs can form a salt bridge?
Both α-keratin and tropocollagen have helical secondary structure. How do these molecules differ in (a) amino acid composition and (b) three-dimensional structure?