Modest influence of FRET chromophores on the properties of unfolded proteins. - Wikidata - awgldk - TriplyDB

Modest influence of FRET chromophores on the properties of unfolded proteins.

Modest influence of FRET chromophores on the properties of unfolded proteins.

http://www.wikidata.org/entity/Q34310142

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Balanced Protein-Water Interactions Improve Properties of Disordered Proteins and Non-Specific Protein Association Quantitative interpretation of FRET experiments via molecular simulation: force field and validation.Finding Our Way in the Dark Proteome.Consistent View of Polypeptide Chain Expansion in Chemical Denaturants from Multiple Experimental Methods.Probing the Action of Chemical Denaturant on an Intrinsically Disordered Protein by Simulation and Experiment.Nonlinear reconstruction of single-molecule free-energy surfaces from univariate time series.Sequence- and Temperature-Dependent Properties of Unfolded and Disordered Proteins from Atomistic Simulations.

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P2860

Modest influence of FRET chromophores on the properties of unfolded proteins.

http://www.wikidata.org/entity/Q34310142

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2014 nî lūn-bûn

@nan

2014 թուականի Հոկտեմբերին հրատարակուած գիտական յօդուած

@hyw

2014 թվականի հոտեմբերին հրատարակված գիտական հոդված

@hy

2014年の論文

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2014年論文

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2014年論文

@zh-hant

2014年論文

@zh-hk

2014年論文

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2014年論文

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2014年论文

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name

Modest influence of FRET chromophores on the properties of unfolded proteins.

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Modest influence of FRET chromophores on the properties of unfolded proteins.

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Modest influence of FRET chromophores on the properties of unfolded proteins.

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type

label

Modest influence of FRET chromophores on the properties of unfolded proteins.

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Modest influence of FRET chromophores on the properties of unfolded proteins.

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Modest influence of FRET chromophores on the properties of unfolded proteins.

@nl

prefLabel

Modest influence of FRET chromophores on the properties of unfolded proteins.

@ast

Modest influence of FRET chromophores on the properties of unfolded proteins.

@en

Modest influence of FRET chromophores on the properties of unfolded proteins.

@nl

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J.BPJ.2014.07.071

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Biophysical Journal

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Modest influence of FRET chromophores on the properties of unfolded proteins.

@en

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Gül H Zerze

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Jeetain Mittal

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P2860

Structural Ensemble of an Intrinsically Disordered Polypeptide

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Assessing the accuracy of physical models used in protein-folding simulations: quantitative evidence from long molecular dynamics simulations

Structural heterogeneity and quantitative FRET efficiency distributions of polyprolines through a hybrid atomistic simulation and Monte Carlo approach

Solution NMR structure of the cold-shock protein from the hyperthermophilic bacterium Thermotoga maritima

Solution structure of the N-terminal zinc binding domain of HIV-1 integrase

Dictionary of protein secondary structure: pattern recognition of hydrogen-bonded and geometrical features

GROMACS 4: Algorithms for Highly Efficient, Load-Balanced, and Scalable Molecular Simulation

Structure, function, and folding of phosphoglycerate kinase are strongly perturbed by macromolecular crowding

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