Skip to main content
NCBI home page
Biophysical Journal logoLink to Biophysical Journal
. 1976 Aug;16(8):931–938. doi: 10.1016/S0006-3495(76)85743-8

Numerical inversion of the Perrin equations for rotational and translational diffusion constants by iterative techniques.

A K Wright, J E Baxter
PMCID: PMC1334918  PMID: 938731

Abstract

An iterative numerical technique is presented which allows the semiaxes for prolate and oblate ellipsoids to be determined from the Perrin equations for rotational and translational diffusion constants. The use of this inversion technique is illustrated by application to the proteins: lysozyme, bovine serum albumin, human transferrin, and bovine rhodopsin solubilized in digitonin.

Full text

PDF
931

Selected References

These references are in PubMed. This may not be the complete list of references from this article.

  1. CREETH J. M. The use of the Gouy diffusiometer with dilute protein solutions; an assessment of the accuracy of the method. Biochem J. 1952 Apr;51(1):10–17. doi: 10.1042/bj0510010. [DOI] [PMC free article] [PubMed] [Google Scholar]
  2. Cummins H. Z., Carlson F. D., Herbert T. J., Woods G. Translational and rotational diffusion constants of tobacco mosaic virus from Rayleigh linewidths. Biophys J. 1969 Apr;9(4):518–546. doi: 10.1016/S0006-3495(69)86402-7. [DOI] [PMC free article] [PubMed] [Google Scholar]
  3. Dubin S. B., Lunacek J. H., Benedek G. B. Observation of the spectrum of light scattered by solutions of biological macromolecules. Proc Natl Acad Sci U S A. 1967 May;57(5):1164–1171. doi: 10.1073/pnas.57.5.1164. [DOI] [PMC free article] [PubMed] [Google Scholar]
  4. HUBBARD R. The molecular weight of rhodopsin and the nature of the rhodopsin-digitonin complex. J Gen Physiol. 1954 Jan 20;37(3):381–399. doi: 10.1085/jgp.37.3.381. [DOI] [PMC free article] [PubMed] [Google Scholar]
  5. Raj T., Flygare W. H. Diffusion studies of bovine serum albumin by quasielastic light scattering. Biochemistry. 1974 Jul 30;13(16):3336–3340. doi: 10.1021/bi00713a024. [DOI] [PubMed] [Google Scholar]
  6. Roberts R., Makey D. G., Seal U. S. Human transferrin. Molecular weight and sedimentation properties. J Biol Chem. 1966 Nov 10;241(21):4907–4913. [PubMed] [Google Scholar]
  7. Rosseneu-Motreff M. Y., Soetewey F., Lamote R., Peeters H. Dielectric study of the urea denaturation of delipidated and relipidated bovine serum albumin. Biopolymers. 1973 Jun;12(6):1259–1267. doi: 10.1002/bip.1973.360120606. [DOI] [PubMed] [Google Scholar]
  8. Rosseneu-Motreff M. Y., Soetewey F., Lamote R., Peeters H. Size and shape determination of apotransferrin and transferrin monomers. Biopolymers. 1971 Jun;10(6):1039–1048. doi: 10.1002/bip.360100610. [DOI] [PubMed] [Google Scholar]
  9. Squire P. G., Moser P., O'Konski C. T. The hydrodynamic properties of bovine serum albumin monomer and dimer. Biochemistry. 1968 Dec;7(12):4261–4272. doi: 10.1021/bi00852a018. [DOI] [PubMed] [Google Scholar]
  10. Strackee L. Rotational diffusion of rhodopsin-digitonin micelles studied by transient photodichroism. Biophys J. 1971 Sep;11(9):728–738. doi: 10.1016/S0006-3495(71)86250-1. [DOI] [PMC free article] [PubMed] [Google Scholar]
  11. Wright A. K. A study of rhodopsin-detergent micelles by transient electric birefringence. Biophys Chem. 1976 Mar;4(2):199–202. doi: 10.1016/0301-4622(76)85010-7. [DOI] [PubMed] [Google Scholar]
  12. Wright A. K., Duncan R. C., Beekman K. A. A numerical inversion of the perrin equations for rotational diffusion constants for ellipsoids of revolution by iterative techniques. Biophys J. 1973 Aug;13(8):795–803. doi: 10.1016/S0006-3495(73)86025-4. [DOI] [PMC free article] [PubMed] [Google Scholar]
  13. Wright A. K. Letter: Ellipsoid models for rotational diffusion of rhodopsin in a digitonin micelle and in the visual receptor membrane. Biophys J. 1974 Mar;14(3):243–245. doi: 10.1016/S0006-3495(74)85912-6. [DOI] [PMC free article] [PubMed] [Google Scholar]
  14. Wright A. K., Thompson M. R. Hydrodynamic structure of bovine serum albumin determined by transient electric birefringence. Biophys J. 1975 Feb;15(2 Pt 1):137–141. doi: 10.1016/s0006-3495(75)85797-3. [DOI] [PMC free article] [PubMed] [Google Scholar]

Articles from Biophysical Journal are provided here courtesy of The Biophysical Society

RESOURCES