Folding of beta-sheet proteins

Abstract

In the past year, interesting new information concerning various aspects of the folding process of beta-sheet proteins has been gleaned. Kinetic and equilibrium folding intermediates have been characterized. Studies of extensively denatured states and of model peptide fragments have enabled important steps to be taken towards an understanding of the initiation of the folding process of beta-sheet proteins. Site-directed mutagenesis has been used in combination with various probes to monitor folding events.