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Molecular hinges in protein folding: the urea-denaturated state of apomyoglobin

Authors :
Schwarzinger, Stephan
Wright, Peter E.
Dyson, H. Jane
Source :
Biochemistry. Oct 22, 2002, Vol. 41 Issue 42, p12681, 6 p.
Publication Year :
2002

Abstract

Research has been conducted on the unfolded apomyoglobin. The NMR characterization of this apomyoglobin denaturated in urea has been carried out in investigating polypeptide's behavior under denaturing conditions and the details are presented.

Subjects

Subjects :
Biochemistry -- Research
Protein folding -- Physiological aspects
Urea -- Physiological aspects
Polypeptides -- Physiological aspects
Nuclear magnetic resonance spectroscopy -- Usage
Biological sciences
Chemistry

Details

ISSN :
00062960
Volume :
41
Issue :
42
Database :
Gale General OneFile
Journal :
Biochemistry
Publication Type :
Academic Journal
Accession number :
edsgcl.93787617

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