Biochemistry
9th Edition
ISBN: 9781319114671
Author: Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.
Publisher: W. H. Freeman
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Question
Chapter 3, Problem 3P
Interpretation Introduction
Interpretation:
The reason for the peptide bonds on the carboxyl side of S-aminoethyl derivatives is vulnerable to hydrolysis by trypsin should be determined.
Concept introduction:
Cysteine is a sulphur-containing amino acid. It takes place in keratins and other proteins usually in the form of cysteine and is a component of many enzymes.
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Check out a sample textbook solutionStudents have asked these similar questions
- Keto counterparts. Name the a-ketoacida-ketoacid that is formed by
the transamination of each of the following amino acids: Co,
a. Alanine
b. Leucine
c. Aspartate
d. Phenylalanine
e. Glutamate
f. Tyrosine
Ionization State of Histidine.Each ionizable group of an amino acid can exist in one of two states, charged or neutral. The electric charge on the functional group is determined by the relationship between its pKa and the pH of the solution. This relationship is described by the Henderson-Hasselbalch equation.
1.Histidine has three ionizable functional groups. Write the equilibrium equations for its three ion-izationsand assign the proper pKa for each ionization. Draw the structure of histidine in each ionization state.What is the net charge on the histidine molecule in each ionization state?
2.Which structure drawn in (1) corresponds to theionization state of histidine at pH 1, 4, 8, and12?Note that the ionization state can be approximated by treating each ionizable group independently.
3.What is the net charge of histidine at pH 1, 4, 8, and 12? For each pH, will histidine migrate to-ward the anode (+) or cathode (-) when placed in an electric field?
Be sure to answer all parts.
Give the amino acid sequence of an octapeptide that contains the amino acids Thr, Phe, Ile (2 equiv),
Asp, Cys, Val, Leu, and forms the following fragments when partially hydrolyzed with HCl:
Thr-Ile-Phe, Phe-Ile-Asp-Val, and Asp-Val-Cys-Leu.
Chapter 3 Solutions
Biochemistry
Ch. 3 - Prob. 1PCh. 3 - Prob. 2PCh. 3 - Prob. 3PCh. 3 - Prob. 4PCh. 3 - Prob. 5PCh. 3 - Prob. 6PCh. 3 - Prob. 7PCh. 3 - Prob. 8PCh. 3 - Prob. 9PCh. 3 - Prob. 10P
Ch. 3 - Prob. 11PCh. 3 - Prob. 12PCh. 3 - Prob. 13PCh. 3 - Prob. 14PCh. 3 - Prob. 15PCh. 3 - Prob. 16PCh. 3 - Prob. 17PCh. 3 - Prob. 18PCh. 3 - Prob. 19PCh. 3 - Prob. 20PCh. 3 - Prob. 21PCh. 3 - Prob. 22PCh. 3 - Prob. 23PCh. 3 - Prob. 24PCh. 3 - Prob. 25PCh. 3 - Prob. 26PCh. 3 - Prob. 27PCh. 3 - Prob. 28PCh. 3 - Prob. 29PCh. 3 - Prob. 30PCh. 3 - Prob. 31P
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