Redesigning the folding energetics of a model three-helix bundle protein by site-directed mutagenesis.

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Stabilization of partially folded states in protein folding/misfolding transitions by hydrostatic pressure.Effects of conducting and blocking ions on the structure and stability of the potassium channel KcsA.

P2860

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P2860

Redesigning the folding energetics of a model three-helix bundle protein by site-directed mutagenesis.

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http://www.wikidata.org/entity/Q44710643

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2003 nî lūn-bûn

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2003年の論文

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2003年学术文章

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2003年学术文章

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2003年学术文章

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2003年学术文章

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Redesigning the folding energe ...... by site-directed mutagenesis.

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Redesigning the folding energe ...... by site-directed mutagenesis.

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Item

label

Redesigning the folding energe ...... by site-directed mutagenesis.

@en

Redesigning the folding energe ...... by site-directed mutagenesis.

@nl

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Redesigning the folding energe ...... by site-directed mutagenesis.

@en

Redesigning the folding energe ...... by site-directed mutagenesis.

@nl

P1476

Redesigning the folding energe ...... by site-directed mutagenesis.

@en

P2093

Alex Chapeaurouge

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

Dahabada H J Lopes

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

Gavin A Manderson

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

Jonas S Johansson

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

Sérgio T Ferreira

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P2860

Effect of cavity-creating mutations in the hydrophobic core of chymotrypsin inhibitor 2

Computer-based redesign of a protein folding pathway

The interpretation of protein structures: total volume, group volume distributions and packing density

Pressure denaturation of beta-lactoglobulin. Different stabilities of isoforms A and B, and an investigation of the Tanford transition.

Photoincorporation of 4,4'-bis(1-anilino-8-naphthalenesulfonic acid) into the apical domain of GroEL: specific information from a nonspecific probe.

High pressure effects on protein structure and function.

Tuning the free-energy landscape of a WW domain by temperature, mutation, and truncation.

Cold denaturation and 2H2O stabilization of a staphylococcal nuclease mutant.

Probing the contribution of internal cavities to the volume change of protein unfolding under pressure

PABMB Lecture. Protein dynamics, folding and misfolding: from basic physical chemistry to human conformational diseases.

P304

10991-10996

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

P31

scholarly article

P356

10.1074/JBC.M308174200

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

P407

English

P433

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

P478

279

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

P577

2003-12-30T00:00:00Z

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P698

14701847

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

P921

protein folding

Redesigning the folding energetics of a model three-helix bundle protein by site-directed mutagenesis.

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P2860

P2860

Redesigning the folding energetics of a model three-helix bundle protein by site-directed mutagenesis.

description

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type

label

prefLabel

P1433

P1476

P2093

P2860

P304

P31

P356

P407

P433

P478

P577

P698

P921

P356

P1433

P1476

P2093

P2860

P304

P31

P356

P407

P433

P478

P577

P698

P921