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Chapter 21 719

Copyright © 2017 Pearson Education, Inc.

43.

The data from treatment with Edman’s reagent and carboxypeptidase A identify the first and last amino acids.

Leu

Ser

The data from cleavage with cyanogen bromide identify the position of Met and identify the other amino

acids in the pentapeptide and tripeptide but not their order.

Leu

Met

Ser

Arg, Lys, Tyr

Arg, Phe

cleavage with cyanogen bromide

The data from treatment with trypsin put the remaining amino acids in the correct positions.

Leu

Met

Ser

Tyr

Lys

Arg

Arg

Phe

44.

a.

Trypsin cleaves at Arg and Lys. There are two possible primary structures:

Val

@

Gly

@

Asp

@

Lys

@

Leu

@

Glu

@

Pro

@

Ala

@

Arg

@

Ala

@

Leu

@

Gly

@

Asp

or

Leu

@

Glu

@

Pro

@

Ala

@

Arg

@

Val

@

Gly

@

Asp

@

Lys

@

Ala

@

Leu

@

Gly

@

Asp

The two possible primary structures can be distinguished by Edman’s reagent. Edman’s reagent will

release Val in one case and Leu in the other.

b.

Trypsin cleaves at Arg and Lys. There are two possible primary structures:

Ala

@

Glu

@

Pro

@

Arg

@

Ala

@

Met

@

Gly

@

Lys

@

Val

@

Leu

@

Gly

@

Glu

or

Ala

@

Met

@

Gly

@

Lys

@

Ala

@

Glu

@

Pro

@

Arg

@

Val

@

Leu

@

Gly

@

Glu

The two possible primary structures can be distinguished by treatment with cyanogen bromide.

Cyanogen bromide will cleave one of the possible polypeptides into two hexamers and the other into a

dimer and a decamer.

45.

a.

74 amino acids/3.6 amino acids per turn of the helix

=

20.6 turns of the helix

20.6 × 5.4 Å =

110 Å

in an

a

-helix (5.4 Å is the repeat distance of the

a

-helix.)

b.

74 amino acids × 3.5 Å =

260 Å

in fully extended polypeptide chain

46.

It would fold so that its nonpolar residues are on the outside of the protein in contact with the nonpolar

membrane and its polar residues are on the inside of the protein.

47.

A protein folds to maximize the number of polar groups on the surface of the protein and the number of

nonpolar groups on the inside of the protein.

a.

A cigar-shaped protein has the greatest surface area to volume ratio, so it has the highest percentage of

polar amino acids.

b.

A subunit of a hexamer has the smallest percentage of polar amino acids, because part of the surface of

the subunit can be on the inside of the hexamer and, therefore, have nonpolar amino acids on its surface.