Folding of beta-sheet proteins.
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.
Department of Chemistry, Linköping University, Sweden.
U
U
Carlsson
B H
BH
Jonsson
D000596:Amino Acids / Q000737:chemistry; D007700:Kinetics; D015335:Molecular Probes; D011487:Protein Conformation; D011489:Protein Denaturation; D015202:Protein Engineering; D017510:Protein Folding; D017433:Protein Structure, Secondary
D000596:Amino Acids; D015335:Molecular Probes