New methods to measure residues coevolution in proteins. - Wikidata - wikimedia - TriplyDB

New methods to measure residues coevolution in proteins.

New methods to measure residues coevolution in proteins.

http://www.wikidata.org/entity/Q33911907

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Emerging Computational Methods for the Rational Discovery of Allosteric Drugs.Coupled mutation finder: a new entropy-based method quantifying phylogenetic noise for the detection of compensatory mutations Improving the thermostability of alpha-amylase by combinatorial coevolving-site saturation mutagenesis.A new ensemble coevolution system for detecting HIV-1 protein coevolution.Quantum coupled mutation finder: predicting functionally or structurally important sites in proteins using quantum Jensen-Shannon divergence and CUDA programming.New Measurement for Correlation of Co-evolution Relationship of Subsequences in Protein.Protein sites with more coevolutionary connections tend to evolve slower, while more variable protein families acquire higher coevolutionary connections.New measurement for correlation of co-evolution relationship of subsequences in protein.Comparative analysis of sequence covariation methods to mine evolutionary hubs: examples from selected GPCR families.Targeting functional motifs of a protein family.

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New methods to measure residues coevolution in proteins.

http://www.wikidata.org/entity/Q33911907

description

2011 nî lūn-bûn

@nan

2011 թուականի Մայիսին հրատարակուած գիտական յօդուած

@hyw

2011 թվականի մայիսին հրատարակված գիտական հոդված

@hy

2011年の論文

@ja

2011年論文

@yue

2011年論文

@zh-hant

2011年論文

@zh-hk

2011年論文

@zh-mo

2011年論文

@zh-tw

2011年论文

@wuu

name

New methods to measure residues coevolution in proteins.

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New methods to measure residues coevolution in proteins.

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type

label

New methods to measure residues coevolution in proteins.

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New methods to measure residues coevolution in proteins.

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prefLabel

New methods to measure residues coevolution in proteins.

@ast

New methods to measure residues coevolution in proteins.

@en

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1471-2105-12-206

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BMC Bioinformatics

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New methods to measure residues coevolution in proteins.

@en

P2093

Hongyun Gao

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

Jialiang Yang

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

Jun Wang

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

Yongchao Dou

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

P2860

Structural plasticity in a remodeled protein-protein interface

PDBsum more: new summaries and analyses of the known 3D structures of proteins and nucleic acids

Amino acid substitution matrices from protein blocks

Pfam: clans, web tools and services

The crystal structure of cystathionine gamma-synthase from Nicotiana tabacum reveals its substrate and reaction specificity

Channeling of ammonia in glucosamine-6-phosphate synthase

Evolutionarily conserved pathways of energetic connectivity in protein families

Evolution of protein sequences and structures.

Coevolving protein residues: maximum likelihood identification and relationship to structure.

Persistently conserved positions in structurally similar, sequence dissimilar proteins: roles in preserving protein fold and function.

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1471-2105-12-206

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10.1186/1471-2105-12-206

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