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Backbone additivity in the transfer model of protein solvation.

Backbone additivity in the transfer model of protein solvation.

http://www.wikidata.org/entity/Q33844255

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Residual structure in unfolded proteins Quantitative characterization of local protein solvation to predict solvent effects on protein structure.Solubility and aggregation of Gly(5) in water.Effects of geometry and chemistry on hydrophobic solvation.Multibody correlations in the hydrophobic solvation of glycine peptides Protein denaturants at aqueous-hydrophobic interfaces: self-consistent correlation between induced interfacial fluctuations and denaturant stability at the interface.Synergy in protein-osmolyte mixtures.Peptide conformational preferences in osmolyte solutions: transfer free energies of decaalanine.Fast Calculations of Electrostatic Solvation Free Energy from Reconstructed Solvent Density using proximal Radial Distribution Functions Force field-dependent solution properties of glycine oligomers Problems of robustness in Poisson-Boltzmann binding free energies Further optimization of a hybrid united-atom and coarse-grained force field for folding simulations: Improved backbone hydration and interactions between charged side chains.Protein collapse driven against solvation free energy without H-bonds.Solvation free energy of the peptide group: its model dependence and implications for the additive-transfer free-energy model of protein stability Solvation free energies of alanine peptides: the effect of flexibility.Examining the assumptions underlying continuum-solvent models.Reconciling the understanding of 'hydrophobicity' with physics-based models of proteins.Reaching new levels of realism in modeling biological macromolecules in cellular environments.Empirical Optimization of Interactions between Proteins and Chemical Denaturants in Molecular Simulations.Solvation Thermodynamics of Oligoglycine with Respect to Chain Length and Flexibility.The contribution of electrostatic interactions to the collapse of oligoglycine in water.Ionic strength independence of charge distributions in solvation of biomolecules.Note: On the universality of proximal radial distribution functions of proteins.Using a FRET Library with Multiple Probe Pairs To Drive Monte Carlo Simulations of α-Synuclein.Peptide Solubility Limits: Backbone and Side-Chain Interactions.Intramolecular Interactions Overcome Hydration to Drive the Collapse Transition of Gly15.Thermodynamics of Conformational Transitions in a Disordered Protein Backbone Model

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P2860

Backbone additivity in the transfer model of protein solvation.

http://www.wikidata.org/entity/Q33844255

description

2010 nî lūn-bûn

@nan

2010 թուականի Մայիսին հրատարակուած գիտական յօդուած

@hyw

2010 թվականի մայիսին հրատարակված գիտական հոդված

@hy

2010年の論文

@ja

2010年論文

@yue

2010年論文

@zh-hant

2010年論文

@zh-hk

2010年論文

@zh-mo

2010年論文

@zh-tw

2010年论文

@wuu

name

Backbone additivity in the transfer model of protein solvation.

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Backbone additivity in the transfer model of protein solvation.

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type

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Backbone additivity in the transfer model of protein solvation.

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Backbone additivity in the transfer model of protein solvation.

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Backbone additivity in the transfer model of protein solvation.

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Protein Science

P1476

Backbone additivity in the transfer model of protein solvation.

@en

P2093

B Montgomery Pettitt

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

Char Y Hu

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

D Wayne Bolen

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Gillian C Lynch

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Hironori Kokubo

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P2860

The structure of proteins; two hydrogen-bonded helical configurations of the polypeptide chain

A backbone-based theory of protein folding

All-atom empirical potential for molecular modeling and dynamics studies of proteins

The molecular mechanism of stabilization of proteins by TMAO and its ability to counteract the effects of urea

Living with water stress: evolution of osmolyte systems

Structure and energetics of the hydrogen-bonded backbone in protein folding.

Urea, but not guanidinium, destabilizes proteins by forming hydrogen bonds to the peptide group.

Counteraction of urea destabilization of protein structure by methylamine osmoregulatory compounds of elasmobranch fishes.

A naturally occurring protective system in urea-rich cells: mechanism of osmolyte protection of proteins against urea denaturation.

Trimethylamine-N-oxide counteracts urea effects on rabbit muscle lactate dehydrogenase function: a test of the counteraction hypothesis.

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1011-1022

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scholarly article

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10.1002/PRO.378

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5

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19

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20306490

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