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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Chapter 3, Problem 25P
Interpretation Introduction
Interpretation:
Two methods that could be applied to the study of hydrogen-deuterium exchange rates in proteins should be mentioned and explained.
Concept introduction:
Hydrogen-deuterium exchange is a reaction by which a covalently bonded hydrogen atoms are replaced by deuterium atoms. This method is commonly used for the solvent accessibility of proteins and thereby determining the tertiary structure of the protein. The protons on amide groups are exchangeable.
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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?
Peptide mass determination. You have isolated a proteinfrom the bacterium E. coli and seek to confirm its identityby trypsin digestion and mass spectrometry. Determinationof the masses of several peptide fragments has enabled youto deduce the identity of the protein. However, there is adiscrepancy with one of the peptide fragments, whichyou believe should have the sequence MLNSFK and an(M 1 H)1 value of 739.38. In your experiments, yourepeat edly obtain an (M 1 H)1 value of 767.38. What isthe cause of this discrepancy and what does it tell youabout the region of the protein from which this peptide isderived?
Sedimenting spheres. What is the dependence of the sedimentation coefficient s of a spherical protein on its mass?How much more rapidly does an 80 -kDa protein sedimentthan does a 40-kDa protein?
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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