Long Time Protein Dynamics

The long time dynamics (time scale greater than picoseconds) of macromolecules in solution are governed by diffusion. In water the protein configuration diffuses in a complex conformational energy landscape with a large number of energy valleys separated by energy barriers (Young et al. 1991). Local dynamics in polypeptides, as described by NMR relaxation or fluorescence anisotropy, are very sensitive to the structure of the residues, to the inter-residue correlations and to the sequence cooperativity. This dependence of conformation and dynamics on local features is responsible for the great variety of protein biological functions observed in nature.