Literature DB >> 16272443

A protein molecule in a mixed solvent: the preferential binding parameter via the Kirkwood-Buff theory.

Ivan L Shulgin1, Eli Ruckenstein.   

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Year:  2005        PMID： 16272443      PMCID： PMC1367075          DOI： 10.1529/biophysj.105.074112

Source DB:  PubMed          Journal:  Biophys J        ISSN： 0006-3495            Impact factor:   4.033


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  15 in total

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Review 2.  Water as ligand: preferential binding and exclusion of denaturants in protein unfolding.

Authors:  S N Timasheff
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Review 3.  THERMODYNAMIC ANALYSIS OF MULTICOMPONENT SOLUTIONS.

Authors:  E F CASASSA; H EISENBERG
Journal:  Adv Protein Chem       Date:  1964

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5.  The Kirkwood-Buff theory and the effect of cosolvents on biochemical reactions.

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Journal:  J Chem Phys       Date:  2004-11-08       Impact factor: 3.488

6.  A contribution to the theory of preferential interaction coefficients.

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Review 7.  Control of protein stability and reactions by weakly interacting cosolvents: the simplicity of the complicated.

Authors:  S N Timasheff
Journal:  Adv Protein Chem       Date:  1998

Review 8.  Analysis of effects of salts and uncharged solutes on protein and nucleic acid equilibria and processes: a practical guide to recognizing and interpreting polyelectrolyte effects, Hofmeister effects, and osmotic effects of salts.

Authors:  M T Record; W Zhang; C F Anderson
Journal:  Adv Protein Chem       Date:  1998

9.  Thermodynamic characterization of interactions of native bovine serum albumin with highly excluded (glycine betaine) and moderately accumulated (urea) solutes by a novel application of vapor pressure osmometry.

Authors:  W Zhang; M W Capp; J P Bond; C F Anderson; M T Record
Journal:  Biochemistry       Date:  1996-08-13       Impact factor: 3.162

10.  Preferential solvation of bovine serum albumin in aqueous guanidine hydrochloride.

Authors:  M E Noelken; S N Timasheff
Journal:  J Biol Chem       Date:  1967-11-10       Impact factor: 5.157
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2.  Chemical potential derivatives and preferential interaction parameters in biological systems from Kirkwood-Buff theory.

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3.  An analysis of the molecular origin of osmolyte-dependent protein stability.

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Review 4.  Recent applications of Kirkwood-Buff theory to biological systems.

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Journal:  Cell Biochem Biophys       Date:  2007-11-28       Impact factor: 2.194

5.  SANS/SAXS study of the BSA solvation properties in aqueous urea solutions via a global fit approach.

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6.  Fluctuation theory of molecular association and conformational equilibria.

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7.  Ion counting from explicit-solvent simulations and 3D-RISM.

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8.  Thermodynamic and structural basis for relaxation of specificity in protein-DNA recognition.

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  8 in total

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