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Assessing accumulated solvent near a macromolecular solute by preferential interaction coefficients

Assessing accumulated solvent near a macromolecular solute by preferential interaction coefficients

http://www.wikidata.org/entity/Q34177978

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Recent applications of Kirkwood-Buff theory to biological systems Biomolecular electrostatics and solvation: a computational perspective Preferential binding effects on protein structure and dynamics revealed by coarse-grained Monte Carlo simulation.Comparison of the effect of water release on the interaction of the Saccharomyces cerevisiae TATA binding protein (TBP) with "TATA Box" sequences composed of adenosine or inosine.Estimating hydration changes upon biomolecular reactions from osmotic stress, high pressure, and preferential hydration experiments.Chemical potential derivatives and preferential interaction parameters in biological systems from Kirkwood-Buff theory.Microcalorimetric study of thermal unfolding of lysozyme in water/glycerol mixtures: an analysis by solvent exchange model.

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Assessing accumulated solvent near a macromolecular solute by preferential interaction coefficients

http://www.wikidata.org/entity/Q34177978

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2002 nî lūn-bûn

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2002 թուականի Յունիսին հրատարակուած գիտական յօդուած

@hyw

2002 թվականի հունիսին հրատարակված գիտական հոդված

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2002年の論文

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2002年論文

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2002年論文

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2002年論文

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2002年論文

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2002年論文

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2002年论文

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name

Assessing accumulated solvent ...... ntial interaction coefficients

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Assessing accumulated solvent ...... ntial interaction coefficients

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Assessing accumulated solvent ...... ntial interaction coefficients

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S0006-3495(02)75629-4

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Biophysical Journal

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Assessing accumulated solvent ...... ntial interaction coefficients

@en

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Karen E S Tang

http://www.w3.org/2001/XMLSchema#string

Victor A Bloomfield

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P2860

Direct observation of protein solvation and discrete disorder with experimental crystallographic phases

Steric exclusion is the principal source of the preferential hydration of proteins in the presence of polyethylene glycols

Stabilization of protein structure by sugars.

Solvation study of the non-specific lipid transfer protein from wheat by intermolecular NOEs with water and small organic molecules.

A global model of the protein-solvent interface.

Grand canonical Monte Carlo molecular and thermodynamic predictions of ion effects on binding of an oligocation (L8+) to the center of DNA oligomers.

Interpretation of preferential interaction coefficients of nonelectrolytes and of electrolyte ions in terms of a two-domain model

Excluded volume in solvation: sensitivity of scaled-particle theory to solvent size and density

Monte Carlo description of oligoelectrolyte properties of DNA oligomers: range of the end effect and the approach of molecular and thermodynamic properties to the polyelectrolyte limits

THERMODYNAMIC ANALYSIS OF MULTICOMPONENT SOLUTIONS.

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2876-2891

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scholarly article

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10.1016/S0006-3495(02)75629-4

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6

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2002-06-01T00:00:00Z

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