Conformational Dynamics of apo-GlnBP Revealed by Experimental and Computational Analysis.

about

Linking time-series of single-molecule experiments with molecular dynamics simulations by machine learning.

P2860

Q55040516-DDDBFA3C-224E-4941-9D2E-BEC70DF476DF

P2860

Conformational Dynamics of apo-GlnBP Revealed by Experimental and Computational Analysis.

Item

http://www.wikidata.org/entity/Q36161231

description

2016 nî lūn-bûn

@nan

2016年の論文

@ja

2016年論文

@yue

2016年論文

@zh-hant

2016年論文

@zh-hk

2016年論文

@zh-mo

2016年論文

@zh-tw

2016年论文

@wuu

2016年论文

@zh

2016年论文

@zh-cn

name

Conformational Dynamics of apo-GlnBP Revealed by Experimental and Computational Analysis.

@ast

Conformational Dynamics of apo-GlnBP Revealed by Experimental and Computational Analysis.

@en

type

Item

label

Conformational Dynamics of apo-GlnBP Revealed by Experimental and Computational Analysis.

@ast

Conformational Dynamics of apo-GlnBP Revealed by Experimental and Computational Analysis.

@en

prefLabel

Conformational Dynamics of apo-GlnBP Revealed by Experimental and Computational Analysis.

@ast

Conformational Dynamics of apo-GlnBP Revealed by Experimental and Computational Analysis.

@en

P1476

Conformational Dynamics of apo-GlnBP Revealed by Experimental and Computational Analysis

@en

P2093

Jianwei Liu

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

Lu Zhang

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

Maili Liu

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

Shaowen Wu

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

Xu Zhang

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

Yitao Feng

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

Zhijun Liu

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

P2860

Structure-based design of robust glucose biosensors using aThermotoga maritimaperiplasmic glucose-binding protein

Open-to-closed transition in apo maltose-binding protein observed by paramagnetic NMR

Crystal structures of the choline/acetylcholine substrate-binding protein ChoX from Sinorhizobium meliloti in the liganded and unliganded-closed states

The crystal structure of glutamine-binding protein from Escherichia coli

The structure of glutamine-binding protein complexed with glutamine at 1.94 A resolution: comparisons with other amino acid binding proteins

A role for both conformational selection and induced fit in ligand binding by the LAO protein

Quantitatively characterizing the ligand binding mechanisms of choline binding protein using Markov state model analysis

The role of dynamic conformational ensembles in biomolecular recognition

The differences in the microenvironment of the two tryptophan residues of the glutamine-binding protein from Escherichia coli shed light on the binding properties and the structural dynamics of the protein.

A practical guide to single-molecule FRET

P304

13990-13994

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

P31

scholarly article

P356

10.1002/ANIE.201606613

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

P407

English

P433

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

P478

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

P50

Xuhui Huang

Xin Gao

Wenning Wang

P577

2016-10-12T00:00:00Z

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

P698

27730716

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

Conformational Dynamics of apo-GlnBP Revealed by Experimental and Computational Analysis.

about

P2860

P2860

Conformational Dynamics of apo-GlnBP Revealed by Experimental and Computational Analysis.

description

name

type

label

prefLabel

P1433

P1476

P2093

P2860

P304

P31

P356

P407

P433

P478

P50

P577

P698

P356

P1433

P1476

P2093

P2860

P304

P31

P356

P407

P433

P478

P50

P577

P698