Ontology highlight
ABSTRACT:
SUBMITTER: Ladurner AG
PROVIDER: S-EPMC21100 | biostudies-literature | 1998 Jul
REPOSITORIES: biostudies-literature
Ladurner A G AG Itzhaki L S LS Daggett V V Fersht A R AR
Proceedings of the National Academy of Sciences of the United States of America 19980701 15
Experimental data from protein engineering studies and NMR spectroscopy have been used by theoreticians to develop algorithms for helix propensity and to benchmark computer simulations of folding pathways and energy landscapes. Molecular dynamic simulations of the unfolding of chymotrypsin inhibitor 2 (CI2) have provided detailed structural models of the transition state ensemble for unfolding/folding of the protein. We now have used the simulated transition state structures to design faster fol ...[more]