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Chapter D3 - Macromolecular diffusion

from Part D - Hydrodynamics

Published online by Cambridge University Press:  05 November 2012

Igor N. Serdyuk ,
Nathan R. Zaccai  and
Joseph Zaccai
Igor N. Serdyuk
Affiliation:
Institute of Protein Research, Moscow
Nathan R. Zaccai
Affiliation:
University of Bristol
Joseph Zaccai
Affiliation:
Institut de Biologie Structurale, Grenoble
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Summary

Historical review

1850

T. Graham observed that egg albumin diffuses much more slowly than common compounds such as salt or sugar. In 1861 he used dialysis to separate mixtures of slowly and rapidly diffusing solutes, and made quantitative measurements of diffusion on many substances. On the basis of this work he classified matter in terms of colloids and crystalloids.

1855

A. Fick, in the equations now known as his first and second laws, defined a diffusion coefficient (D) to describe the flow of a solute down its concentration gradient. J. Stefan (1879) and L. Boltzmann (1894) developed mathematical integral forms of the second law, opening the way for the experimental determination of diffusion coefficients by various methods.

1905–1906

A. Einstein, W. Sutherland and M. von Smoluchowski determined that steady-state solutions of Fick's equations have a direct analogy in heat flow along a temperature gradient, and established mathematical relations between diffusion and frictional coefficients in Brownian motion. In 1905, W. Sutherland used a value of D calculated by J. Stefan from data collected by T. Graham, to obtain a molecular weight of 33000 for egg albumin (the true value is about 45000).

1926

L. Mandelshtam recognised that the translational diffusion coefficient of macromolecules could be obtained from the spectrum of scattered light. However, the lack of spatial coherence and the non-monochromatic nature of conventional light sources rendered such experiments impossible until 1964 when H. Cummins, N. Knable and Y. Yeh used an optical-mixing technique to resolve spectrally the light scattered from dilute suspensions of polystyrene latex spheres.

Type
Chapter
Information
Methods in Molecular Biophysics
Structure, Dynamics, Function
 , pp. 318 - 338
Publisher: Cambridge University Press
Print publication year: 2007

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References

Gosting, L. J. (1956). Measurement and interpretation of diffusion coefficient of proteins. Adv. Prot. Chem., 11, 429–554.CrossRefGoogle Scholar
Einstein, A. (1956). Investigations on the Theory of the Brownian Movement, ed. Furth, R., transl. by Cowper, A. D.. New York: Dover Publications, Inc.Google Scholar
Berg, H. C. (1983). Random Walks in Biology. Princeton: Princeton University Press.Google Scholar
Berg, H. C. (1983). Random Walks in Biology.Princeton: Princeton University Press.Google Scholar
Gosting, L. J. (1956). Measurement and interpretation of diffusion coefficient of proteins. Adv. Prot. Chem., 11, 429–554.CrossRefGoogle Scholar
Axelrod, D., Koppel, D. E., Schlessinger, J., Elson, E., and Webb, W. W. (1976). Mobility measurement by analysis of fluorescence photobleaching recovery kinetics. Biophys. J., 16, 1055–1069.CrossRefGoogle ScholarPubMed
Kucik, D. F., Elson, E., and Sheetz, M. P. (1989). Forward transport of glycoproteins on leading lamellipoda in locomoting cells. Nature, 340, 315–316.CrossRefGoogle Scholar
Lee, G. M., Ishihara, A., and Jacobson, K. A. (1991). Direct observation of Brownian motion of lipids in a membrane. Proc. Natl. Acad. Sci. USA, 88, 6274–6278.CrossRefGoogle ScholarPubMed
Rowe, A. J. (1977). The concentration dependence of transport processes: A general description applicable to the sedimentation, translation diffusion, and viscosity coefficients of macromolecular solutes. Biopolymers, 16, 2595–2611.CrossRefGoogle Scholar
Harding, S. E., and Johnson, P. (1985). The concentration dependence of macromolecular parameters. Biochem. J., 231, 543–547.CrossRefGoogle ScholarPubMed
Teller, D., Swanson, E., and Haen, C. (1979). The translation friction coefficients of proteins. Meth. Enzymol., 61, 103–124.Google Scholar
Venable, R. M., and Pastor, R. W. (1988). Frictional models for stochastic simulations of proteins. Biopolymers, 27, 1001–1014.CrossRefGoogle ScholarPubMed
Garcia de la Torre, J. (2001). Hydration from hydrodynamics. General consideration and applications to bead modelling to globular proteins. Biophys. Chem., 93, 159–170.CrossRefGoogle Scholar
Zhou, H.-X. (2001). A unified picture of protein hydration: prediction of hydrodynamic properties from known structures. Biophys. Chem., 93, 171–179.CrossRefGoogle ScholarPubMed
Gosting, L. J. (1956). Measurement and interpretation of diffusion coefficient of proteins. Adv. Prot. Chem., 11, 429–554.CrossRefGoogle Scholar
Einstein, A. (1956). Investigations on the theory of the Brownian movement, ed. Furth, R., transl. by Cowper, A. D.. New York: Dover Publications, Inc.Google Scholar
Gosting, L. J. (1956). Measurement and interpretation of diffusion coefficient of proteins. Adv. Prot. Chem., 11, 429–554.CrossRefGoogle Scholar
Einstein, A. (1956). Investigations on the Theory of the Brownian Movement, ed. Furth, R., transl. by Cowper, A. D.. New York: Dover Publications, Inc.Google Scholar
Berg, H. C. (1983). Random Walks in Biology. Princeton: Princeton University Press.Google Scholar
Berg, H. C. (1983). Random Walks in Biology.Princeton: Princeton University Press.Google Scholar
Gosting, L. J. (1956). Measurement and interpretation of diffusion coefficient of proteins. Adv. Prot. Chem., 11, 429–554.CrossRefGoogle Scholar
Axelrod, D., Koppel, D. E., Schlessinger, J., Elson, E., and Webb, W. W. (1976). Mobility measurement by analysis of fluorescence photobleaching recovery kinetics. Biophys. J., 16, 1055–1069.CrossRefGoogle ScholarPubMed
Kucik, D. F., Elson, E., and Sheetz, M. P. (1989). Forward transport of glycoproteins on leading lamellipoda in locomoting cells. Nature, 340, 315–316.CrossRefGoogle Scholar
Lee, G. M., Ishihara, A., and Jacobson, K. A. (1991). Direct observation of Brownian motion of lipids in a membrane. Proc. Natl. Acad. Sci. USA, 88, 6274–6278.CrossRefGoogle ScholarPubMed
Rowe, A. J. (1977). The concentration dependence of transport processes: A general description applicable to the sedimentation, translation diffusion, and viscosity coefficients of macromolecular solutes. Biopolymers, 16, 2595–2611.CrossRefGoogle Scholar
Harding, S. E., and Johnson, P. (1985). The concentration dependence of macromolecular parameters. Biochem. J., 231, 543–547.CrossRefGoogle ScholarPubMed
Teller, D., Swanson, E., and Haen, C. (1979). The translation friction coefficients of proteins. Meth. Enzymol., 61, 103–124.Google Scholar
Venable, R. M., and Pastor, R. W. (1988). Frictional models for stochastic simulations of proteins. Biopolymers, 27, 1001–1014.CrossRefGoogle ScholarPubMed
Garcia de la Torre, J. (2001). Hydration from hydrodynamics. General consideration and applications to bead modelling to globular proteins. Biophys. Chem., 93, 159–170.CrossRefGoogle Scholar
Zhou, H.-X. (2001). A unified picture of protein hydration: prediction of hydrodynamic properties from known structures. Biophys. Chem., 93, 171–179.CrossRefGoogle ScholarPubMed
Gosting, L. J. (1956). Measurement and interpretation of diffusion coefficient of proteins. Adv. Prot. Chem., 11, 429–554.CrossRefGoogle Scholar
Einstein, A. (1956). Investigations on the theory of the Brownian movement, ed. Furth, R., transl. by Cowper, A. D.. New York: Dover Publications, Inc.Google Scholar

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