Ontology highlight
ABSTRACT:
SUBMITTER: Wallqvist A
PROVIDER: S-EPMC1300450 | biostudies-other | 1999 Sep
REPOSITORIES: biostudies-other
Wallqvist A A Lavoie T A TA Chanatry J A JA Covell D G DG Carey J J
Biophysical journal 19990901 3
A previously published computational procedure was used to identify cooperative folding units within tryptophan repressor. The theoretical results predict the existence of distinct stable substructures in the protein chain for the monomer and the dimer. The predictions were compared with experimental data on structure and folding of the repressor and its proteolytic fragments and show excellent agreement for the dimeric form of the protein. The results suggest that the monomer, the structure of ...[more]