Simple, yet powerful methodologies for conformational sampling of proteins.

Simple, yet powerful methodologies for conformational sampling of proteins.

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http://www.wikidata.org/entity/Q38346856
Structural dissimilarity sampling with dynamically self-guiding selection.Preferential binding effects on protein structure and dynamics revealed by coarse-grained Monte Carlo simulation.Advanced molecular dynamics simulation methods for kinase drug discovery.Enhanced sampling simulations to construct free-energy landscape of protein-partner substrate interaction.Sparsity-weighted outlier FLOODing (OFLOOD) method: Efficient rare event sampling method using sparsity of distribution.Variability of the Cyclin-Dependent Kinase 2 Flexibility Without Significant Change in the Initial Conformation of the Protein or Its Environment; a Computational Study.Temperature-shuffled parallel cascade selection molecular dynamics accelerates the structural transitions of proteins.Significance of NS5B Substitutions in Genotype 1b Hepatitis C Virus Evaluated by Bioinformatics Analysis.
P2860

Simple, yet powerful methodologies for conformational sampling of proteins.

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http://www.wikidata.org/entity/Q38346856
description
2015 nî lūn-bûn
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2015年の論文
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2015年論文
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2015年論文
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2015年論文
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2015年論文
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2015年論文
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2015年论文
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2015年论文
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name
Simple, yet powerful methodologies for conformational sampling of proteins.
@en
type
label
Simple, yet powerful methodologies for conformational sampling of proteins.
@en
prefLabel
Simple, yet powerful methodologies for conformational sampling of proteins.
@en
P1433
P1476
P2093
P2860
P304
P31
P356
P407
P433
P478
P50
P577
P698
P356
P1433
P1476
Simple, yet powerful methodologies for conformational sampling of proteins
@en
P2093
P2860
P304
P31
P356
P407
P433
P478
P50
P577
P698