Kinetically trapped metastable intermediate of a disulfide-deficient mutant of the starch-binding domain of glucoamylase.

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Survey of the year 2009: applications of isothermal titration calorimetry.

P2860

Q37820930-45AF2C64-0207-4AE0-B751-F7B2A495CDFE

P2860

Kinetically trapped metastable intermediate of a disulfide-deficient mutant of the starch-binding domain of glucoamylase.

Item

http://www.wikidata.org/entity/Q42635817

description

2009 nî lūn-bûn

@nan

2009年の論文

@ja

2009年論文

@yue

2009年論文

@zh-hant

2009年論文

@zh-hk

2009年論文

@zh-mo

2009年論文

@zh-tw

2009年论文

@wuu

2009年论文

@zh

2009年论文

@zh-cn

name

Kinetically trapped metastable ...... inding domain of glucoamylase.

@en

Kinetically trapped metastable ...... inding domain of glucoamylase.

@nl

type

Item

label

Kinetically trapped metastable ...... inding domain of glucoamylase.

@en

Kinetically trapped metastable ...... inding domain of glucoamylase.

@nl

prefLabel

Kinetically trapped metastable ...... inding domain of glucoamylase.

@en

Kinetically trapped metastable ...... inding domain of glucoamylase.

@nl

P1476

Kinetically trapped metastable ...... inding domain of glucoamylase.

@en

P2093

Akiyoshi Tanaka

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

Hayuki Sugimoto

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

Hideo Miyake

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

Miho Nakaura

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

Shigenori Nishimura

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

Shuichi Karita

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

P2860

Solution structure of the granular starch binding domain of glucoamylase from Aspergillus niger by nuclear magnetic resonance spectroscopy

Solution structure of the granular starch binding domain of Aspergillus niger glucoamylase bound to beta-cyclodextrin

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A partially folded intermediate species of the beta-sheet protein apo-pseudoazurin is trapped during proline-limited folding

Probing the folding intermediate of Rd-apocyt b562 by protein engineering and infrared T-jump

Demonstration of a low-energy on-pathway intermediate in a fast-folding protein by kinetics, protein engineering, and simulation

Role of the molten globule state in protein folding.

Kinetic evidence for an on-pathway intermediate in the folding of cytochrome c.

The 28-111 disulfide bond constrains the alpha-lactalbumin molten globule and weakens its cooperativity of folding.

A tightly packed hydrophobic cluster directs the formation of an off-pathway sub-millisecond folding intermediate in the alpha subunit of tryptophan synthase, a TIM barrel protein

P304

1715-1723

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scholarly article

P356

10.1002/PRO.188

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

P478

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

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2009-08-01T00:00:00Z

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

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26295536

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19530230

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2776959

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

Kinetically trapped metastable intermediate of a disulfide-deficient mutant of the starch-binding domain of glucoamylase.

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P2860

P2860

Kinetically trapped metastable intermediate of a disulfide-deficient mutant of the starch-binding domain of glucoamylase.

description

name

type

label

prefLabel

P1433

P1476

P2093

P2860

P304

P31

P356

P433

P478

P577

P5875

P698

P932

P356

P1433

P1476

P2093

P2860

P304

P31

P356

P433

P478

P577

P5875

P698

P932