4. The study of conditions that optimize the association of proteins in solution guides the design of protocols for formation of large crystals. It is important to characterize protein dimerization (2P - 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 (I) of the rate constant (k) of dimerization in aqueous solution of an ionic protein P at 298 K: P2), I/Io 0.0100 0.0150 0.0200 0.0250 0.0300 0.0350 k/ko 8.10 13.30 20.50 27.80 38.10 52.00 Note: Io = 1 mol/L, ko = 1 L/(mol•s). (a) What effect is this, and what is its physical origin? (b) Determine the charge state of this protein, P. Note: One needs to use all data points.

4. The study of conditions that optimize the association of proteins in solution guides the design of protocols for formation of large crystals. It is important to characterize protein dimerization (2P - 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 (I) of the rate constant (k) of dimerization in aqueous solution of an ionic protein P at 298 K: P2), I/Io 0.0100 0.0150 0.0200 0.0250 0.0300 0.0350 k/ko 8.10 13.30 20.50 27.80 38.10 52.00 Note: Io = 1 mol/L, ko = 1 L/(mol•s). (a) What effect is this, and what is its physical origin? (b) Determine the charge state of this protein, P. Note: One needs to use all data points.

Chemistry

10th Edition

ISBN:9781305957404

Author:Steven S. Zumdahl, Susan A. Zumdahl, Donald J. DeCoste

Publisher:Steven S. Zumdahl, Susan A. Zumdahl, Donald J. DeCoste

Chapter1: Chemical Foundations

Section: Chapter Questions

Problem 1RQ: Define and explain the differences between the following terms. a. law and theory b. theory and...

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