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Chapter D9 - Viscosity

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

1846

J. L. Poiseuille produced a theory of liquid flow in a capillary. Based on this theory, W. Ostwald (1933) and L. Ubbelohde (1936) invented viscometers and introduced them into physical and chemical practice. Later, the instruments were named after them.

1906

A. Einstein was the first to treat the viscosity of suspensions of rigid spherical particles that are large relative to the size of the solvent molecules. He showed that the specific viscosity of the solution is proportional to the volume fraction of the solution occupied by the particles and does not depend on the absolute size of the spheres.

1932

H. Staudinger proposed using the intrinsic viscosity to determine the molecular mass of polymers. He found that the dependence of the intrinsic viscosity on the molecular mass for a homologous series of polymers can be expressed by a simple formula of the type [η] ≈ Mα. It became understood later (H. Mark, R. Houwink, W. Kuhn and H. Kuhn) that the constant α is related to the molecular conformation of the macromolecules in solution.

1962

B. H. Zimm and D. M. Crothers proposed an original design for a rotational viscometer that operates at low velocity gradients and which has been very useful for measurements on asymmetric structures such as DNA, fibrous proteins and rod-like viruses.

1985

M. A. Haney invented a ‘differential viscometer’ which measures the relative viscosity directly.

Type
Chapter
Information
Methods in Molecular Biophysics
Structure, Dynamics, Function
 , pp. 466 - 480
Publisher: Cambridge University Press
Print publication year: 2007

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References

Harding, S. E. (1997). The intrinsic viscosity of biological macromolecules. Progress in measurement, interpretation and application to structure in dilute solution. Prog. Biophys. Mol. Biol., 68, 207–262.CrossRefGoogle ScholarPubMed
Zhou, H.-X. (1995). Calculation of translational friction and intrinsic viscosity. I. General formulation for arbitrary shaped particles. Biophysical J., 69, 2286–2297.CrossRefGoogle Scholar
Zhou, H.-X. (1995). Calculation of translational friction and intrinsic viscosity. II. Application to globular proteins. Biophysical J., 69, 2298–2303.CrossRefGoogle ScholarPubMed
Brenner, H. (1974). Rheology of a dilute suspension of axisymmetric Brownian particles. Int. I. Multiphase Flow, 1, 195–341.CrossRefGoogle Scholar
Allison, S. A. (1999). Low Reynolds number transport properties of axisymmetric particles employing stick and slip boundary conditions. Macromolecules, 32, 5304–5312.CrossRefGoogle Scholar
Cantor, C., and Schimmel, P. (1980). Biophysical Chemistry. Part II. Technique for the study of Biological Structure and Function. San Francisco: W.H. Freeman and Co.Google Scholar
Dutta, R. K., Hammons, K., Willibey, B., and Haney, M. A. (1991). Analysis of protein denaturation by high-performance continuous differential viscometry. J. Chromatogr., 536, 113–121.CrossRefGoogle ScholarPubMed
Tsvetkov, V. N., Eskin, V. E., and Frenkel, S. Ya. (1971). Structure of Macromolecules in Solution (translated from Russian), Volume 1. Chapter 7. Boston, UK: National Lending Library for Science and Technology.Google Scholar
Tanford, C., Kawahara, K., and Lapanije, S. (1967). Proteins as a random coils. Intrinsic viscosity and sedimentation coefficients in concentrated guanidine hydrochloride. J. Amer. Chem. Soc., 89, 729–736.CrossRefGoogle Scholar
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
Crothers, D. M., and Zimm, B. H. (1965). Viscosity and sedimentation of the DNA from bacteriophages T2 and T7 and the relation to molecular weight. J. Mol. Biol., 12, 527–536.CrossRefGoogle ScholarPubMed
Doty, P., Bradbury, J. H., and Holtzer, A. M. (1956). Polypeptides. IV. The molecular weight, configruation and association of poly-γ-glutamate in various solvents. J. Am. Chem. Soc., 78, 947–954.CrossRefGoogle Scholar
Yangi, J. T. (1961). The viscosity of macromolecules in relation to molecular conformation. Adv. Protein. Chem., 16, 323–400.CrossRefGoogle Scholar
Tanford, C. (1968). Protein denaturation. Adv. Protein Chem., 23, 121–282.CrossRefGoogle ScholarPubMed
Holde, K. (1985). Physical Biochemistry. Englewood Cliffs, NJ: Prentice-Hall.Google Scholar
Harding, S. E. (1997). The intrinsic viscosity of biological macromolecules. Progress in measurement, interpretation and application to structure in dilute solution. Prog. Biophys. Mol. Biol., 68, 207–262.CrossRefGoogle ScholarPubMed
Zhou, H.-X. (1995). Calculation of translational friction and intrinsic viscosity. I. General formulation for arbitrary shaped particles. Biophysical J., 69, 2286–2297.CrossRefGoogle Scholar
Zhou, H.-X. (1995). Calculation of translational friction and intrinsic viscosity. II. Application to globular proteins. Biophysical J., 69, 2298–2303.CrossRefGoogle ScholarPubMed
Brenner, H. (1974). Rheology of a dilute suspension of axisymmetric Brownian particles. Int. I. Multiphase Flow, 1, 195–341.CrossRefGoogle Scholar
Allison, S. A. (1999). Low Reynolds number transport properties of axisymmetric particles employing stick and slip boundary conditions. Macromolecules, 32, 5304–5312.CrossRefGoogle Scholar
Cantor, C., and Schimmel, P. (1980). Biophysical Chemistry. Part II. Technique for the study of Biological Structure and Function. San Francisco: W.H. Freeman and Co.Google Scholar
Dutta, R. K., Hammons, K., Willibey, B., and Haney, M. A. (1991). Analysis of protein denaturation by high-performance continuous differential viscometry. J. Chromatogr., 536, 113–121.CrossRefGoogle ScholarPubMed
Tsvetkov, V. N., Eskin, V. E., and Frenkel, S. Ya. (1971). Structure of Macromolecules in Solution (translated from Russian), Volume 1. Chapter 7. Boston, UK: National Lending Library for Science and Technology.Google Scholar
Tanford, C., Kawahara, K., and Lapanije, S. (1967). Proteins as a random coils. Intrinsic viscosity and sedimentation coefficients in concentrated guanidine hydrochloride. J. Amer. Chem. Soc., 89, 729–736.CrossRefGoogle Scholar
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
Crothers, D. M., and Zimm, B. H. (1965). Viscosity and sedimentation of the DNA from bacteriophages T2 and T7 and the relation to molecular weight. J. Mol. Biol., 12, 527–536.CrossRefGoogle ScholarPubMed
Doty, P., Bradbury, J. H., and Holtzer, A. M. (1956). Polypeptides. IV. The molecular weight, configruation and association of poly-γ-glutamate in various solvents. J. Am. Chem. Soc., 78, 947–954.CrossRefGoogle Scholar
Yangi, J. T. (1961). The viscosity of macromolecules in relation to molecular conformation. Adv. Protein. Chem., 16, 323–400.CrossRefGoogle Scholar
Tanford, C. (1968). Protein denaturation. Adv. Protein Chem., 23, 121–282.CrossRefGoogle ScholarPubMed
Holde, K. (1985). Physical Biochemistry. Englewood Cliffs, NJ: Prentice-Hall.Google Scholar

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  • Viscosity
  • Igor N. Serdyuk, Institute of Protein Research, Moscow, Nathan R. Zaccai, University of Bristol, Joseph Zaccai, Institut de Biologie Structurale, Grenoble
  • Book: Methods in Molecular Biophysics
  • Online publication: 05 November 2012
  • Chapter DOI: https://doi.org/10.1017/CBO9780511811166.022
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Save book to Dropbox

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  • Viscosity
  • Igor N. Serdyuk, Institute of Protein Research, Moscow, Nathan R. Zaccai, University of Bristol, Joseph Zaccai, Institut de Biologie Structurale, Grenoble
  • Book: Methods in Molecular Biophysics
  • Online publication: 05 November 2012
  • Chapter DOI: https://doi.org/10.1017/CBO9780511811166.022
Available formats
×

Save book to Google Drive

To save content items to your account, please confirm that you agree to abide by our usage policies. If this is the first time you use this feature, you will be asked to authorise Cambridge Core to connect with your account. Find out more about saving content to Google Drive.

  • Viscosity
  • Igor N. Serdyuk, Institute of Protein Research, Moscow, Nathan R. Zaccai, University of Bristol, Joseph Zaccai, Institut de Biologie Structurale, Grenoble
  • Book: Methods in Molecular Biophysics
  • Online publication: 05 November 2012
  • Chapter DOI: https://doi.org/10.1017/CBO9780511811166.022
Available formats
×