P18C.7 The study of conditions that optimize the association of proteins in solution guides the design of protocols for formation of large crystals that are amenable to analysis by X-ray diffraction techniques. It is important to characterize protein dimerization because the process is considered to be the rate-determining step in the growth of crystals of many proteins. Consider the variation with ionic strength of the rate constant at 298 K of dimerization in aqueous solution of a cationic protein P: I 0.0100 0.0150 0.0200 0.0250 0.0300 0.0350 8.10 13.30 20.50 27.80 38.10 52.00 What can be deduced about the charge of P?
P18C.7 The study of conditions that optimize the association of proteins in solution guides the design of protocols for formation of large crystals that are amenable to analysis by X-ray diffraction techniques. It is important to characterize protein dimerization because the process is considered to be the rate-determining step in the growth of crystals of many proteins. Consider the variation with ionic strength of the rate constant at 298 K of dimerization in aqueous solution of a cationic protein P: I 0.0100 0.0150 0.0200 0.0250 0.0300 0.0350 8.10 13.30 20.50 27.80 38.10 52.00 What can be deduced about the charge of P?
Chemistry
10th Edition
ISBN:9781305957404
Author:Steven S. Zumdahl, Susan A. Zumdahl, Donald J. DeCoste
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Chapter1: Chemical Foundations
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![P18C.7 The study of conditions that optimize the association of proteins in
solution guides the design of protocols for formation of large crystals that
are amenable to analysis by X-ray diffraction techniques. It is important to
characterize protein dimerization because the process is considered to be the
rate-determining step in the growth of crystals of many proteins. Consider the
variation with ionic strength of the rate constant at 298 K of dimerization in
aqueous solution of a cationic protein P:
I
0.0100
0.0150
0.0200
0.0250
0.0300
0.0350
8.10
13.30
20.50
27.80
38.10
52.00
What can be deduced about the charge of P?](/v2/_next/image?url=https%3A%2F%2Fcontent.bartleby.com%2Fqna-images%2Fquestion%2F542f0811-e5e1-4a87-bc81-5860553d8874%2F0ca30292-b8ae-4be4-a3d7-9402b28490e5%2Flasjhfq.png&w=3840&q=75)
Transcribed Image Text:P18C.7 The study of conditions that optimize the association of proteins in
solution guides the design of protocols for formation of large crystals that
are amenable to analysis by X-ray diffraction techniques. It is important to
characterize protein dimerization because the process is considered to be the
rate-determining step in the growth of crystals of many proteins. Consider the
variation with ionic strength of the rate constant at 298 K of dimerization in
aqueous solution of a cationic protein P:
I
0.0100
0.0150
0.0200
0.0250
0.0300
0.0350
8.10
13.30
20.50
27.80
38.10
52.00
What can be deduced about the charge of P?
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