Literature DB >> 17588257

The effective hard particle model provides a simple, robust, and broadly applicable description of nonideal behavior in concentrated solutions of bovine serum albumin and other nonassociating proteins.

Allen P Minton1.   

Abstract

Published data on the concentration dependence of osmotic pressure of solutions of bovine serum albumin in 0.15 M NaCl at concentrations up to greater than 400 g/L are shown to be described to within experimental uncertainty by a simple one-parameter model in which protein molecules are represented by effective hard spherical particles. The volume of the effective hard particle reflects both steric and electrostatic repulsion and thus varies with pH and ionic strength. The pH dependence of the effective volume is shown to agree well with that previously obtained from analysis of the concentration dependence of sedimentation equilibrium and static light scattering. (c) 2007 Wiley-Liss, Inc.

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Year:  2007        PMID: 17588257     DOI: 10.1002/jps.20964

Source DB:  PubMed          Journal:  J Pharm Sci        ISSN: 0022-3549            Impact factor:   3.534


  26 in total

1.  Effective hard particle model for the osmotic pressure of highly concentrated binary protein solutions.

Authors:  Allen P Minton
Journal:  Biophys J       Date:  2008-01-22       Impact factor: 4.033

2.  Static light scattering from concentrated protein solutions II: experimental test of theory for protein mixtures and weakly self-associating proteins.

Authors:  Cristina Fernández; Allen P Minton
Journal:  Biophys J       Date:  2009-03-04       Impact factor: 4.033

3.  Automated measurement of the static light scattering of macromolecular solutions over a broad range of concentrations.

Authors:  Cristina Fernández; Allen P Minton
Journal:  Anal Biochem       Date:  2008-06-27       Impact factor: 3.365

4.  Small-angle neutron scattering characterization of monoclonal antibody conformations and interactions at high concentrations.

Authors:  Eric J Yearley; Isidro E Zarraga; Steven J Shire; Thomas M Scherer; Yatin Gokarn; Norman J Wagner; Yun Liu
Journal:  Biophys J       Date:  2013-08-06       Impact factor: 4.033

5.  Practical considerations over spectral quality in solid state NMR spectroscopy of soluble proteins.

Authors:  Marco Fragai; Claudio Luchinat; Giacomo Parigi; Enrico Ravera
Journal:  J Biomol NMR       Date:  2013-08-30       Impact factor: 2.835

Review 6.  Macromolecular crowding and confinement: biochemical, biophysical, and potential physiological consequences.

Authors:  Huan-Xiang Zhou; Germán Rivas; Allen P Minton
Journal:  Annu Rev Biophys       Date:  2008       Impact factor: 12.981

7.  Critical examination of the colloidal particle model of globular proteins.

Authors:  Prasad S Sarangapani; Steven D Hudson; Ronald L Jones; Jack F Douglas; Jai A Pathak
Journal:  Biophys J       Date:  2015-02-03       Impact factor: 4.033

8.  The fallacy of misplaced concreteness.

Authors:  John Prausnitz
Journal:  Biophys J       Date:  2015-02-03       Impact factor: 4.033

9.  Quantitative characterization of polymer-polymer, protein-protein, and polymer-protein interaction via tracer sedimentation equilibrium.

Authors:  Adedayo A Fodeke; Allen P Minton
Journal:  J Phys Chem B       Date:  2010-08-26       Impact factor: 2.991

10.  Quantitative assessment of the relative contributions of steric repulsion and chemical interactions to macromolecular crowding.

Authors:  Allen P Minton
Journal:  Biopolymers       Date:  2013-04       Impact factor: 2.505

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