BIOCHEMISTRY (HARDBACK) W/ACCESS CODE
BIOCHEMISTRY (HARDBACK) W/ACCESS CODE
6th Edition
ISBN: 9781337194204
Author: GARRETT
Publisher: CENGAGE L
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Chapter 5, Problem 2P

Answers to all problems are at the end of this book. Detailed solutions are available in the Student Solutions Manual, Study Guide, and Problems Book.

Solving the Sequence of an Oligopeptide From Sequence Analysis Data Amino acid analysis of ail oligopeptide seven residues long gave

Chapter 5, Problem 2P, Answers to all problems are at the end of this book. Detailed solutions are available in the Student , example  1

The following fads were observed:

a. Trypsin treatment had no apparent effect.

b. The phenylthiohydantoin released by Lid mini degradation was

Chapter 5, Problem 2P, Answers to all problems are at the end of this book. Detailed solutions are available in the Student , example  2

c. Brief chymotrypsin treatment yielded several products, including a dipeptide and a tetrapeptide. The amino acid composition of the tetrapeptide was Leu, Lyi. and Met.

d. Cyanogen bromide treatment yielded a dipeptide, a tetrapeptide, and free Lys.

What is the amino acid sequence of this heptapeptide?

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Hair grows at a rate of about 20 cm/yr. All this growth is concentrated at the base of the hair fiber, where a-keratin filaments are synthesized inside living epidermal cells and assembled into ropelike structures. Two-chan 14 Protofilament 20-30 A Two-chain Intermediate flament -Protob Protofilament Cross section of a hair The fundamental structural element of a keratin is the a helix, which has 3.6 amino acid residues per turn and a rise of 5.4 A perlum. 54A (36) Amino terminus Carbon Hydrogen Oxygen Nitrogen group Carboxyl terminus Assuming that the biosynthesis of a helical keratin chains is the rate-limiting factor in the growth of hair, calculate the rate at which peptide bonds of a-keratin chains must be synthesized (peptide bonds per second) to account for the observed yearly growth of hair. 0422 rate of peptide bond formation: Income bonds/s
Specific rotation is a measure of a solution's capacity to rotate circularly polarized light. The unfolding of the a helix of a polypeptide to a random conformation is accompanied by a large decrease in specific rotation. Polyglutamate, a polypeptide made up of only 1-Glu residues, has the a helix conformation at pH 3. When researchers raise the pH to 7, there is a large decrease in the specific rotation of the solution. Similarly, polylysine (1.-Lys residues) is an a helix at pH 10, but when researchers lower the pH to 7 the specific rotation also decreases, as shown in the graph. a Helix Specific rotation Poly(Glu) a Helix Random conformation Poly(Lys) Random conformation T + ° 2 4 6 В 10 12 14 PH Complete the statements about the molecular mechanism for these changes in specific rotation. Increasing the pH of a polyglutamate solution from 6 to 7 causes the carboxyl group of each glutamate residue Comed Artwer lose a proton. The negatively charged groups in each glutamate residue…
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