Abstract

Proteins acquire their native structures through conformational dynamics proceeding on a nested hierarchy of temporal and spatial scales. The fastest processes occur within picoseconds while slower reactions involving large parts of a protein may proceed on the time scale of seconds. In some situations during the various steps of the protein folding process parts of the protein undergo transitions between structures of well defined geometries. Such conformational dynamics are addressed in the present studies where we use a cyclic chromo-peptide as a model system.

© 2002 Optical Society of America