Identification of three phases in Onconase refolding.

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Stability and folding of amphibian ribonuclease A superfamily members in comparison with mammalian homologues.Consequences of proline-to-alanine substitutions for the stability and refolding of onconase.

P2860

Q38223315-E89E56F6-AF34-4C4F-B0CD-8E3305197C8A Q44928647-83BA1524-A511-4E40-949B-019EBB05DAA1

P2860

Identification of three phases in Onconase refolding.

Item

http://www.wikidata.org/entity/Q46943394

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2007 nî lūn-bûn

@nan

2007年の論文

@ja

2007年学术文章

@wuu

2007年学术文章

@zh

2007年学术文章

@zh-cn

2007年学术文章

@zh-hans

2007年学术文章

@zh-my

2007年学术文章

@zh-sg

2007年學術文章

@yue

2007年學術文章

@zh-hant

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Identification of three phases in Onconase refolding.

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Identification of three phases in Onconase refolding.

@nl

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Item

label

Identification of three phases in Onconase refolding.

@en

Identification of three phases in Onconase refolding.

@nl

prefLabel

Identification of three phases in Onconase refolding.

@en

Identification of three phases in Onconase refolding.

@nl

P1476

Identification of three phases in Onconase refolding.

@en

P2093

Christian Löw

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

Cindy Schulenburg

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

Maria M Martinez-Senac

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

Ralph Golbik

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

Renate Ulbrich-Hofmann

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

Ulrich Arnold

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

P2860

Refined 1.7 A X-ray crystallographic structure of P-30 protein, an amphibian ribonuclease with anti-tumor activity

WHAT IF: a molecular modeling and drug design program

Ribonuclease A

Cyclophilin and peptidyl-prolyl cis-trans isomerase are probably identical proteins

Collapse and cooperativity in protein folding.

Elementary steps in protein folding.

Role of proline isomerization in folding of ribonuclease A at low temperatures

Study of the "molten globule" intermediate state in protein folding by a hydrophobic fluorescent probe.

Both the fast and slow refolding reactions of ribonuclease A yield native enzyme.

Folding of chymotrypsin inhibitor 2. 1. Evidence for a two-state transition.

P304

5826-5833

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

P31

scholarly article

P356

10.1111/J.1742-4658.2007.06106.X

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

P407

English

P433

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

P478

274

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

P577

2007-10-18T00:00:00Z

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

P5875

5900597

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

P698

17944937

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

P921

refolding

Identification of three phases in Onconase refolding.

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P2860

P2860

Identification of three phases in Onconase refolding.

description

name

type

label

prefLabel

P1433

P1476

P2093

P2860

P304

P31

P356

P407

P433

P478

P577

P5875

P698

P921

P356

P1433

P1476

P2093

P2860

P304

P31

P356

P407

P433

P478

P577

P5875

P698

P921