Mutational analysis of a protein-folding pathway.
The effects of amino-acid replacements on the disulphide-coupled folding pathway of bovine pancreatic trypsin inhibitor have been examined. Replacements at three sites destabilize the native protein relative to the unfolded state, but have different effects on the relative stabilities of the disulphide-bonded folding intermediates, thus allowing the roles of the altered residues during folding to be distinguished.
Goldenberg
D P
DP
Department of Biology, University of Utah, Salt Lake City 84112.
Frieden
R W
RW
Haack
J A
JA
Morrison
T B
TB
D000595:Amino Acid Sequence; D007611:Aprotinin; D007700:Kinetics; D008958:Models, Molecular; D009154:Mutation; D011487:Protein Conformation
D007611:Aprotinin