Hydrophobic interactions accelerate early stages of the folding of BPTI

Biochemistry

Volumn 36, Issue 10, 1997, Pages 2788-2797

  Dadlez, Michal ^a  

^a INSTITUTE OF BIOCHEMISTRY AND BIOPHYSICS   (Poland)

Author keywords

[No Author keywords available]

Indexed keywords

APROTININ;

AMINO ACID SEQUENCE; ARTICLE; CRYSTAL STRUCTURE; DISULFIDE BOND; HIGH PERFORMANCE LIQUID CHROMATOGRAPHY; HYDROPHOBICITY; NUCLEAR MAGNETIC RESONANCE; OXIDATIVE PHOSPHORYLATION; PRIORITY JOURNAL; PROTEIN FOLDING; PROTEIN INTERACTION; PROTEIN STRUCTURE;

ANIMALS; APROTININ; CATTLE; CHROMATOGRAPHY, HIGH PRESSURE LIQUID; CYSTEINE; DISULFIDES; GLUTATHIONE; GLUTATHIONE DISULFIDE; KINETICS; MODELS, MOLECULAR; MUTAGENESIS, SITE-DIRECTED; MUTATION; OXIDATION-REDUCTION; PROTEIN FOLDING; RECOMBINANT PROTEINS; SEQUENCE HOMOLOGY, AMINO ACID;

EID: 0030929829     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi962407f     Document Type: Article

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