The role of a trans-proline in the folding mechanism of ribonuclease T1.

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Identification of Conus peptidylprolyl cis-trans isomerases (PPIases) and assessment of their role in the oxidative folding of conotoxins.FK506-Binding protein 22 from a psychrophilic bacterium, a cold shock-inducible peptidyl prolyl isomerase with the ability to assist in protein folding.

P2860

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P2860

The role of a trans-proline in the folding mechanism of ribonuclease T1.

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http://www.wikidata.org/entity/Q54579024

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1996 nî lūn-bûn

@nan

1996年の論文

@ja

1996年学术文章

@wuu

1996年学术文章

@zh-cn

1996年学术文章

@zh-hans

1996年学术文章

@zh-my

1996年学术文章

@zh-sg

1996年學術文章

@yue

1996年學術文章

@zh

1996年學術文章

@zh-hant

name

The role of a trans-proline in the folding mechanism of ribonuclease T1.

@en

The role of a trans-proline in the folding mechanism of ribonuclease T1.

@nl

type

Item

label

The role of a trans-proline in the folding mechanism of ribonuclease T1.

@en

The role of a trans-proline in the folding mechanism of ribonuclease T1.

@nl

prefLabel

The role of a trans-proline in the folding mechanism of ribonuclease T1.

@en

The role of a trans-proline in the folding mechanism of ribonuclease T1.

@nl

P1476

The role of a trans-proline in the folding mechanism of ribonuclease T1.

@en

P2093

F X Schmid

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L M Mayr

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

O Landt

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

T Schindler

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

U Hahn

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

P2860

MOLSCRIPT: a program to produce both detailed and schematic plots of protein structures

Kinetic analysis of the unfolding and refolding of ribonuclease T1 by a stopped-flow double-mixing technique

Determination and analysis of urea and guanidine hydrochloride denaturation curves

Transient folding intermediates characterized by protein engineering.

Cyclophilin 20 is involved in mitochondrial protein folding in cooperation with molecular chaperones Hsp70 and Hsp60

Consideration of the Possibility that the slow step in protein denaturation reactions is due to cis-trans isomerism of proline residues.

Catalysis of protein folding by prolyl isomerase.

Replacement of proline-76 with alanine eliminates the slowest kinetic phase in thioredoxin folding.

Cis-trans isomerization is rate-determining in the reactivation of denatured human carbonic anhydrase II as evidenced by proline isomerase.

A general method for rapid site-directed mutagenesis using the polymerase chain reaction.

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516-524

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scholarly article

P356

10.1111/J.1432-1033.1996.00516.X

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English

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P478

241

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1996-10-01T00:00:00Z

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14290560

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P698

8917450

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The role of a trans-proline in the folding mechanism of ribonuclease T1.

about

P2860

P2860

The role of a trans-proline in the folding mechanism of ribonuclease T1.

description

name

type

label

prefLabel

P1433

P1476

P2093

P2860

P304

P31

P356

P407

P433

P478

P577

P5875

P698

P356

P1433

P1476

P2093

P2860

P304

P31

P356

P407

P433

P478

P577

P5875

P698