Native-like interactions favored in the unfolded bovine pancreatic trypsin inhibitor have different roles in folding

Biochemistry

Volumn 41, Issue 7, 2002, Pages 2246-2253

  Li, Renhao ^a,b   Battiste, John L ^a,c   Woodward, Clare ^a  

^a UNIVERSITY OF MINNESOTA   (United States)

^b UNIVERSITY OF PENNSYLVANIA   (United States)

^c 3M COMPANY   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

FOLDING KINETICS;

CHEMICAL BONDS; PH EFFECTS; PROTEINS; RATE CONSTANTS; SULFUR COMPOUNDS;

BIOCHEMISTRY;

ALANINE; APROTININ; AROMATIC COMPOUND; CYSTEINE; OLIGOMER; TRYPTOPHAN; TYROSINE;

ARTICLE; CONTROLLED STUDY; DENATURATION; DISULFIDE BOND; MOLECULAR INTERACTION; MOLECULAR STABILITY; NONHUMAN; PH; PRIORITY JOURNAL; PROTEIN CONFORMATION; PROTEIN FOLDING; STRUCTURE ANALYSIS;

ANIMALS; APROTININ; CATTLE; CIRCULAR DICHROISM; GUANIDINE; KINETICS; MUTAGENESIS, SITE-DIRECTED; POINT MUTATION; PROTEIN DENATURATION; PROTEIN FOLDING; THERMODYNAMICS; TRYPSIN INHIBITORS;

ANETHUM GRAVEOLENS; BOVINAE;

EID: 0037133265     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi0116947     Document Type: Article

References (52)