Constructing sequence-dependent protein models using coevolutionary information. - Wikidata - awgldk - TriplyDB

Constructing sequence-dependent protein models using coevolutionary information.

Constructing sequence-dependent protein models using coevolutionary information.

http://www.wikidata.org/entity/Q30009132

about

Sequence co-evolutionary information is a natural partner to minimally-frustrated models of biomolecular dynamics Potts Hamiltonian models of protein co-variation, free energy landscapes, and evolutionary fitness.SMOG 2: A Versatile Software Package for Generating Structure-Based Models.Inferring repeat-protein energetics from evolutionary information.Connecting the Sequence-Space of Bacterial Signaling Proteins to Phenotypes Using Coevolutionary Landscapes.Influences of heterogeneous native contact energy and many-body interactions on the prediction of protein folding mechanisms.Structural propensities of kinase family proteins from a Potts model of residue co-variation.Coevolutionary Landscape of Kinase Family Proteins: Sequence Probabilities and Functional Motifs.

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P2860

Constructing sequence-dependent protein models using coevolutionary information.

http://www.wikidata.org/entity/Q30009132

description

2015 nî lūn-bûn

@nan

2015 թուականի Յուլիսին հրատարակուած գիտական յօդուած

@hyw

2015 թվականի հուլիսին հրատարակված գիտական հոդված

@hy

2015年の論文

@ja

2015年論文

@yue

2015年論文

@zh-hant

2015年論文

@zh-hk

2015年論文

@zh-mo

2015年論文

@zh-tw

2015年论文

@wuu

name

Constructing sequence-dependent protein models using coevolutionary information.

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Constructing sequence-dependent protein models using coevolutionary information.

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type

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Constructing sequence-dependent protein models using coevolutionary information.

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Constructing sequence-dependent protein models using coevolutionary information.

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Constructing sequence-dependent protein models using coevolutionary information.

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Constructing sequence-dependent protein models using coevolutionary information.

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Protein Science

P1476

Constructing sequence-dependent protein models using coevolutionary information.

@en

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Jeffrey K Noel

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Mohit Raghunathan

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Ryan R Cheng

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P2860

Dissecting the specificity of protein-protein interaction in bacterial two-component signaling: orphans and crosstalks

The Protein Data Bank

Toward an outline of the topography of a realistic protein-folding funnel

Direct-coupling analysis of residue coevolution captures native contacts across many protein families

Weak pairwise correlations imply strongly correlated network states in a neural population

Theoretical and experimental demonstration of the importance of specific nonnative interactions in protein folding

Crystal structure of the ribosomal protein S6 from Thermus thermophilus

Three-dimensional structure of the tyrosine kinase c-Src

GROMACS: fast, flexible, and free

Mapping the transition state and pathway of protein folding by protein engineering

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111-122

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scholarly article

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3639772

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10.1002/PRO.2758

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1

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25

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