Conformational Dynamics of the GdmHCl-Induced Molten Globule State of Creatine Kinase Monitored by Hydrogen Exchange and Mass Spectrometry-Reference-Cited by-同舟云学术

Conformational Dynamics of the GdmHCl-Induced Molten Globule State of Creatine Kinase Monitored by Hydrogen Exchange and Mass Spectrometry

Published:2004-04-02 Issue:17 Volume:43 Page:5045-5054
ISSN:0006-2960
Container-title:Biochemistry
language:en
Short-container-title:Biochemistry

Author:

Mazon Hortense¹,Marcillat Olivier¹,Forest Eric¹,Smith David L.¹,Vial Christian¹

Affiliation:

1. UMR CNRS 5013, Biomembranes et enzymes associés, Université Claude Bernard Lyon I, 43, boulevard du 11 Novembre 1918, 69622 Villeurbanne Cedex, France, Laboratoire de spectrométrie de masse des protéines, Institut de Biologie Structurale, CNRS (UMR 5075)/CEA/UJF, 41, rue Jules Horowitz, 38027 Grenoble Cedex, France, and Department of Chemistry, University of Nebraska, Lincoln, Nebraska 68588-0304

Publisher

American Chemical Society (ACS)

Subject

Biochemistry

Link

https://pubs.acs.org/doi/pdf/10.1021/bi049965b

Reference70 articles.

1. Protein folding: Hypotheses and experiments

2. The molten globule state as a clue for understanding the folding and cooperativity of globular-protein structure

3. Evidence for a molten globule state as a general intermediate in protein folding

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