Literature DB >> 9334744

Structure of a kinetic protein folding intermediate by equilibrium amide exchange.

L L Hosszu, C J Craven, M J Parker, M Lorch, J Spencer, A R Clarke, J P Waltho.   

Abstract

A combination of equilibrium amide exchange and kinetic folding data show that the essential features of the complex topology of the N-terminal domain of a thermophilic phosphoglycerate kinase are established on a millisecond or faster timescale, before the rate-limiting step in the folding pathway commences.

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Year:  1997        PMID: 9334744     DOI: 10.1038/nsb1097-801

Source DB:  PubMed          Journal:  Nat Struct Biol        ISSN: 1072-8368


  4 in total

1.  The major transition state in folding need not involve the immobilization of side chains.

Authors:  R A Staniforth; J L Dean; Q Zhong; E Zerovnik; A R Clarke; J P Waltho
Journal:  Proc Natl Acad Sci U S A       Date:  2000-05-23       Impact factor: 11.205

2.  Equilibrium amide hydrogen exchange and protein folding kinetics.

Authors:  Y Bai
Journal:  J Biomol NMR       Date:  1999-09       Impact factor: 2.835

3.  The influence of interdomain interactions on the intradomain motions in yeast phosphoglycerate kinase: a molecular dynamics study.

Authors:  Erika Balog; Monique Laberge; Judit Fidy
Journal:  Biophys J       Date:  2006-12-08       Impact factor: 4.033

Review 4.  DMSO-Quenched H/D-Exchange 2D NMR Spectroscopy and Its Applications in Protein Science.

Authors:  Kunihiro Kuwajima; Maho Yagi-Utsumi; Saeko Yanaka; Koichi Kato
Journal:  Molecules       Date:  2022-06-10       Impact factor: 4.927

  4 in total

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