Quantifying the Intrinsic Conformation Energy Landscape Topography of Proteins with Large-Scale Open-Closed Transition

about

Quantifying the Intrinsic Conformation Energy Landscape Topography of Proteins with Large-Scale Open-Closed Transition

Item

http://www.wikidata.org/entity/Q58805422

description

wetenschappelijk artikel

@nl

наукова стаття, опублікована в серпні 2018

@uk

name

Quantifying the Intrinsic Conf ...... e-Scale Open-Closed Transition

@en

Quantifying the Intrinsic Conf ...... e-Scale Open-Closed Transition

@nl

type

Item

label

Quantifying the Intrinsic Conf ...... e-Scale Open-Closed Transition

@en

Quantifying the Intrinsic Conf ...... e-Scale Open-Closed Transition

@nl

prefLabel

Quantifying the Intrinsic Conf ...... e-Scale Open-Closed Transition

@en

Quantifying the Intrinsic Conf ...... e-Scale Open-Closed Transition

@nl

P1476

Quantifying the Intrinsic Conf ...... e-Scale Open-Closed Transition

@en

P2093

Jin Wang

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

Wen-Ting Chu

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

P2860

A database of macromolecular motions

Conformational transitions of adenylate kinase: switching by cracking

Snapshots of a Y-family DNA polymerase in replication: substrate-induced conformational transitions and implications for fidelity of Dpo4

Structure of the Escherichia coli phosphonate binding protein PhnD and rationally optimized phosphonate biosensors

The closed conformation of a highly flexible protein: the structure of E. coli adenylate kinase with bound AMP and AMPPNP

Three-dimensional structures of the periplasmic lysine/arginine/ornithine-binding protein with and without a ligand

Insights into interfacial activation from an open structure of Candida rugosa lipase

Adenylate kinase motions during catalysis: an energetic counterweight balancing substrate binding

Systematic analysis of domain motions in proteins from conformational change: new results on citrate synthase and T4 lysozyme

A hierarchy of timescales in protein dynamics is linked to enzyme catalysis

P304

1015-1022

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

P31

scholarly article

P356

10.1021/ACSCENTSCI.8B00274

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

P577

2018-08-22T00:00:00Z

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

P698

30159398

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

P932

6107866

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