High-Resolution Mapping of the Folding Transition State of a WW Domain

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The Dependence of Carbohydrate-Aromatic Interaction Strengths on the Structure of the Carbohydrate.Using Cooperatively Folded Peptides To Measure Interaction Energies and Conformational Propensities.Toward a quantitative description of microscopic pathway heterogeneity in protein folding.

P2860

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P2860

High-Resolution Mapping of the Folding Transition State of a WW Domain

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http://www.wikidata.org/entity/Q35924644

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2016 nî lūn-bûn

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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

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High-Resolution Mapping of the Folding Transition State of a WW Domain

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High-Resolution Mapping of the Folding Transition State of a WW Domain

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Item

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High-Resolution Mapping of the Folding Transition State of a WW Domain

@ast

High-Resolution Mapping of the Folding Transition State of a WW Domain

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prefLabel

High-Resolution Mapping of the Folding Transition State of a WW Domain

@ast

High-Resolution Mapping of the Folding Transition State of a WW Domain

@en

P1476

High-Resolution Mapping of the Folding Transition State of a WW Domain

@en

P2093

Houbi Nguyen

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

Kapil Dave

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

Marcus Jäger

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

P2860

The WW domain of Yes-associated protein binds a proline-rich ligand that differs from the consensus established for Src homology 3-binding modules

Structure-function-folding relationship in a WW domain

Markov state model reveals folding and functional dynamics in ultra-long MD trajectories

Comparing Fast Pressure Jump and Temperature Jump Protein Folding Experiments and Simulations.

NMR solution structure of the isolated Apo Pin1 WW domain: comparison to the x-ray crystal structures of Pin1

Phi value versus psi analysis

On the precision of experimentally determined protein folding rates and phi-values

Atomic-level characterization of the structural dynamics of proteins

The osmolyte trimethylamine-N-oxide stabilizes the Fyn SH3 domain without altering the structure of its folding transition state.

Protein folding kinetics beyond the phi value: using multiple amino acid substitutions to investigate the structure of the SH3 domain folding transition state.

P304

1617-1636

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P31

scholarly article

P356

10.1016/J.JMB.2016.02.008

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

P407

English

P433

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

P478

428

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

P50

Jeffery W. Kelly

Martin Gruebele

P577

2016-02-12T00:00:00Z

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P698

26880334

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P932

4835268

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

High-Resolution Mapping of the Folding Transition State of a WW Domain

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P2860

P2860

High-Resolution Mapping of the Folding Transition State of a WW Domain

description

name

type

label

prefLabel

P1433

P1476

P2093

P2860

P304

P31

P356

P407

P433

P478

P50

P577

P698

P932

P356

P1433

P1476

P2093

P2860

P304

P31

P356

P407

P433

P478

P50

P577

P698

P932