Interplay between binding affinity and kinetics in protein-protein interactions.

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Dimension conversion and scaling of disordered protein chains.Fast Calculation of Protein-Protein Binding Free Energies using Umbrella Sampling with a Coarse-Grained Model.

P2860

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P2860

Interplay between binding affinity and kinetics in protein-protein interactions.

Item

http://www.wikidata.org/entity/Q51412572

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2016 nî lūn-bûn

@nan

2016年の論文

@ja

2016年学术文章

@wuu

2016年学术文章

@zh

2016年学术文章

@zh-cn

2016年学术文章

@zh-hans

2016年学术文章

@zh-my

2016年学术文章

@zh-sg

2016年學術文章

@yue

2016年學術文章

@zh-hant

name

Interplay between binding affinity and kinetics in protein-protein interactions.

@en

Interplay between binding affinity and kinetics in protein-protein interactions.

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type

Item

label

Interplay between binding affinity and kinetics in protein-protein interactions.

@en

Interplay between binding affinity and kinetics in protein-protein interactions.

@nl

prefLabel

Interplay between binding affinity and kinetics in protein-protein interactions.

@en

Interplay between binding affinity and kinetics in protein-protein interactions.

@nl

P1476

Interplay between binding affinity and kinetics in protein-protein interactions.

@en

P2093

Huaiqing Cao

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

Yongqi Huang

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

Zhirong Liu

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

P2860

Towards a proteome-scale map of the human protein–protein interaction network

Crystal structure of the p14/MP1 scaffolding complex: how a twin couple attaches mitogen-activated protein kinase signaling to late endosomes

Role of the single cysteine residue, Cys 3, of human and bovine cystatin B (stefin B) in the inhibition of cysteine proteinases

DisProt: the Database of Disordered Proteins

Molecular and cellular analysis of Grb2 SH3 domain mutants: interaction with Sos and dynamin

A decade and a half of protein intrinsic disorder: biology still waits for physics

Intrinsically unstructured proteins: re-assessing the protein structure-function paradigm

Dominant forces in protein folding

Protein folding mediated by solvation: water expulsion and formation of the hydrophobic core occur after the structural collapse

Flexible nets. The roles of intrinsic disorder in protein interaction networks.

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920-933

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scholarly article

P356

10.1002/PROT.25041

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English

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

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2016-03-28T00:00:00Z

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27018856

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Interplay between binding affinity and kinetics in protein-protein interactions.

about

P2860

P2860

Interplay between binding affinity and kinetics in protein-protein interactions.

description

name

type

label

prefLabel

P1433

P1476

P2093

P2860

P304

P31

P356

P407

P433

P478

P577

P698

P356

P1433

P1476

P2093

P2860

P304

P31

P356

P407

P433

P478

P577

P698