Characterization of a molten globule state of bovine carbonic anhydrase. III: Loss of asymmetrical environment of the aromatic residues has a profound effect on both the near- and far-UV CD spectrum

Biochimica et Biophysica Acta - Protein Structure and Molecular Enzymology

Volumn 1430, Issue 1, 1999, Pages 111-118

  Borén, Kristina ^a   Andersson, Peter ^a   Larsson, Marie ^a   Carlsson, Uno ^a  

^a LINKÖPING UNIVERSITY   (Sweden)

Author keywords

Aromatic amino acid; Bovine carbonic anhydrase II; Bovine carbonic anhydrase III; Human carbonic anhydrase I; Human carbonic anhydrase II; Molten globule

Indexed keywords

CARBONATE DEHYDRATASE;

AMINO ACID COMPOSITION; ANIMAL TISSUE; ARTICLE; CATTLE; CIRCULAR DICHROISM; CONTROLLED STUDY; ENZYME STRUCTURE; HUMAN; HUMAN TISSUE; IN VITRO STUDY; MUSCLE; NONHUMAN; PRIORITY JOURNAL; PROTEIN DENATURATION; PROTEIN SECONDARY STRUCTURE; PROTEIN STRUCTURE;

ANIMALS; CARBONIC ANHYDRASES; CATTLE; CIRCULAR DICHROISM; ENZYME STABILITY; GUANIDINE; PROTEIN DENATURATION; PROTEIN FOLDING; PROTEIN STRUCTURE, SECONDARY;

EID: 0033040807     PISSN: 01674838     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0167-4838(98)00283-0     Document Type: Article

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