Predicting protein folding rate change upon point mutation using residue-level coevolutionary information.

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Connecting the Sequence-Space of Bacterial Signaling Proteins to Phenotypes Using Coevolutionary Landscapes.Coevolutionary constraints in the sequence-space of macromolecular complexes reflect their self-assembly pathways.Transiently disordered tails accelerate folding of globular proteins.

P2860

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P2860

Predicting protein folding rate change upon point mutation using residue-level coevolutionary information.

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http://www.wikidata.org/entity/Q51645839

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2015 nî lūn-bûn

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2015年の論文

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2015年学术文章

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2015年学术文章

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2015年学术文章

@zh-cn

2015年学术文章

@zh-hans

2015年学术文章

@zh-my

2015年学术文章

@zh-sg

2015年學術文章

@yue

2015年學術文章

@zh-hant

name

Predicting protein folding rat ...... el coevolutionary information.

@en

Predicting protein folding rat ...... el coevolutionary information.

@nl

type

Item

label

Predicting protein folding rat ...... el coevolutionary information.

@en

Predicting protein folding rat ...... el coevolutionary information.

@nl

prefLabel

Predicting protein folding rat ...... el coevolutionary information.

@en

Predicting protein folding rat ...... el coevolutionary information.

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P1476

Predicting protein folding rat ...... vel coevolutionary information

@en

P2093

Smita Das

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

Sudip Kundu

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

P2860

Statistical mechanics of complex networks

Gapped BLAST and PSI-BLAST: a new generation of protein database search programs

Direct-coupling analysis of residue coevolution captures native contacts across many protein families

Protein folding and misfolding

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

Transition-state structure as a unifying basis in protein-folding mechanisms: contact order, chain topology, stability, and the extended nucleus mechanism.

Insights into protein folding mechanisms from large scale analysis of mutational effects.

The network of stabilizing contacts in proteins studied by coevolutionary data.

Mechanisms of protein folding.

Coevolutionary information, protein folding landscapes, and the thermodynamics of natural selection.

P304

3-8

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P31

scholarly article

P356

10.1002/PROT.24960

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

Saurav Mallik

P577

2015-12-09T00:00:00Z

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P5875

283713098

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P698

26566752

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P921

protein folding

Predicting protein folding rate change upon point mutation using residue-level coevolutionary information.

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P2860

P2860

Predicting protein folding rate change upon point mutation using residue-level coevolutionary information.

description

name

type

label

prefLabel

P1433

P1476

P2093

P2860

P304

P31

P356

P407

P433

P478

P50

P577

P5875

P698

P921

P356

P1433

P1476

P2093

P2860

P304

P31

P356

P407

P433

P478

P50

P577

P5875

P698

P921