On the mechanism of human stefin B folding: I. Comparison to homologous stefin A. Influence of pH and trifluoroethanol on the fast and slow folding phases

Proteins: Structure, Function and Genetics

Volumn 32, Issue 3, 1998, Pages 296-303

  Žerovnik, Eva ^a   Virden, Richard ^b   Jerala, Roman ^c   Turk, Vito ^a   Waltho, Jonathan P ^d  

^a JO EF STEFAN INSTITUTE   (Slovenia)

^b NEWCASTLE UNIVERSITY   (United Kingdom)

^c NATIONAL INSTITUTE OF CHEMISTRY   (Slovenia)

^d UNIVERSITY OF SHEFFIELD   (United Kingdom)

Author keywords

Cystatins; Cysteine proteinase inhibitors; Human stefin B; Kinetics; Protein folding; Stopped flow CD; Trifluoroethanol

Indexed keywords

CYSTATIN; CYSTEINE PROTEINASE INHIBITOR; STEFIN A; STEFIN B; TRIFLUOROETHANOL;

ARTICLE; CIRCULAR DICHROISM; FLUORESCENCE; HYDROPHOBICITY; PH; PRIORITY JOURNAL; PROTEIN CONFORMATION; PROTEIN FOLDING; PROTEIN STRUCTURE; PROTEIN TERTIARY STRUCTURE;

CYSTATINS; FLUORESCENCE; HUMANS; HYDROGEN-ION CONCENTRATION; KINETICS; PROTEIN FOLDING; RECOMBINANT PROTEINS; SPECTRUM ANALYSIS; TRIFLUOROETHANOL;

EID: 0032529366     PISSN: 08873585     EISSN: None     Source Type: Journal    
DOI: 10.1002/(SICI)1097-0134(19980815)32:3<296::AID-PROT5>3.0.CO;2-G     Document Type: Article

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