Changes in side chain packing during apomyoglobin folding characterized by pulsed thiol-disulfide exchange

Nature Structural and Molecular Biology

Volumn 5, Issue 8, 1998, Pages 730-737

  Ha, Jeung Hoi ^a   Loh, Stewart N ^a  

^a SUNY UPSTATE MEDICAL UNIVERSITY   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

5,5' DITHIOBIS(2 NITROBENZOIC ACID); APOMYOGLOBIN; DISULFIDE; MUTANT PROTEIN; MYOGLOBIN; THIOL; THIOMESYLIC ACID METHYL ESTER; UNCLASSIFIED DRUG;

ARTICLE; CHEMICAL REACTION KINETICS; CONTROLLED STUDY; ENERGY TRANSFER; FLUORESCENCE; HYDROGEN BOND; NONHUMAN; NUCLEAR MAGNETIC RESONANCE; PH; PRIORITY JOURNAL; PROTEIN FOLDING; PROTEIN STABILITY; X RAY CRYSTALLOGRAPHY;

AMINO ACIDS, SULFUR; APOPROTEINS; CYSTEINE; CYSTINE; DISULFIDES; DITHIONITROBENZOIC ACID; FLOW INJECTION ANALYSIS; KINETICS; METHYL METHANESULFONATE; MODELS, CHEMICAL; MODELS, MOLECULAR; MUTAGENESIS, SITE-DIRECTED; MYOGLOBIN; PROTEIN DENATURATION; PROTEIN ENGINEERING; PROTEIN FOLDING; SPECTROMETRY, FLUORESCENCE; SULFHYDRYL COMPOUNDS; SULFHYDRYL REAGENTS;

EID: 0031853168     PISSN: 15459993     EISSN: 15459985     Source Type: Journal    
DOI: 10.1038/1436     Document Type: Article

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