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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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?
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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