Disorder drives cooperative folding in a multidomain protein

about

Self-Referential Encoding on Modules of Anticodon Pairs-Roots of the Biological Flow System.Transiently disordered tails accelerate folding of globular proteins.

P2860

Q39224176-1FFF935C-EA99-4DEB-A275-8908AEE2311D Q47995118-BEC70A02-D5EC-4186-A773-E7D63F04FA68

P2860

Disorder drives cooperative folding in a multidomain protein

Item

http://www.wikidata.org/entity/Q37369490

description

article científic

@ca

article scientifique

@fr

articolo scientifico

@it

artigo científico

@pt

bilimsel makale

@tr

scientific article published on 03 October 2016

@en

vedecký článok

@sk

vetenskaplig artikel

@sv

videnskabelig artikel

@da

vědecký článek

@cs

name

Disorder drives cooperative folding in a multidomain protein

@en

Disorder drives cooperative folding in a multidomain protein

@en-gb

Disorder drives cooperative folding in a multidomain protein.

@nl

type

Item

label

Disorder drives cooperative folding in a multidomain protein

@en

Disorder drives cooperative folding in a multidomain protein

@en-gb

Disorder drives cooperative folding in a multidomain protein.

@nl

prefLabel

Disorder drives cooperative folding in a multidomain protein

@en

Disorder drives cooperative folding in a multidomain protein

@en-gb

Disorder drives cooperative folding in a multidomain protein.

@nl

P1154

2-s2.0-84991726416

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

P1433

Proceedings of the National Academy of Sciences of the United States of America

P1476

Disorder drives cooperative folding in a multidomain protein

@en

P2093

Carolina A T F Mendonça

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

Dominika T Gruszka

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

Jane Clarke

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

Jennifer R Potts

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

Judith Hawkhead

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

P2860

Prediction and Functional Analysis of Native Disorder in Proteins from the Three Kingdoms of Life

Staphylococcal biofilm-forming protein has a contiguous rod-like structure

Sequential unfolding of ankyrin repeats in tumor suppressor p16

The folding of an enzyme. I. Theory of protein engineering analysis of stability and pathway of protein folding

Cooperative folding of intrinsically disordered domains drives assembly of a strong elongated protein

Biophysical characterisation of the small ankyrin repeat protein myotrophin.

Apparent two-state tendamistat folding is a sequential process along a defined route.

Prepaying the entropic cost for allosteric regulation in KIX

Allostery within a transcription coactivator is predominantly mediated through dissociation rate constants

Titin: properties and family relationships.

P304

11841-11846

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

P31

scholarly article

P356

10.1073/PNAS.1608762113

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

P407

English

P433

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

P478

113

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

P50

Fiona Whelan

Emanuele Paci

P5530

12465540

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

P577

2016-10-03T00:00:00Z

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

P6179

1049093724

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

P698

27698144

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

P921

protein folding

P932

5081646

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

P953

107524/