On the nature of conformational openings: Native and unfolded-state hydrogen and thiol-disulfide exchange studies of ferric aquomyoglobin

Journal of Molecular Biology

Volumn 314, Issue 1, 2001, Pages 153-166

  Feng, Zhaoyang ^a   Butler, Mark C ^a   Alam, Steven L ^b   Loh, Stewart N ^a  

^a State University of New York Upstate Medical University: College of Medicine   (United States)

^b UNIVERSITY OF UTAH SCHOOL OF MEDICINE   (United States)

Author keywords

Dynamics; Local structural fluctuations; Packing; Protein folding; Side chain

Indexed keywords

5,5' DITHIOBIS(2 NITROBENZOIC ACID); AMIDE; APOMYOGLOBIN; FERRIC AQUOMYOLOBIN; HEME; HYDROGEN; MESYLIC ACID METHYL ESTER; MYOGLOBIN; PROTEIN; THIOL DERIVATIVE; THIOL DISULFIDE; UNCLASSIFIED DRUG;

ARTICLE; CHEMICAL REACTION; DENATURATION; ENERGY; KINETICS; MOLECULAR MODEL; PRIORITY JOURNAL; PROTEIN CONFORMATION; PROTEIN FOLDING; PROTEIN STRUCTURE; STRUCTURE ANALYSIS; THEORY; WHALE;

CETACEA; PHYSETER CATODON;

EID: 0035900542     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1006/jmbi.2001.5117     Document Type: Article

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