HYDRONMR: Prediction of NMR relaxation of globular proteins from atomic-level structures and hydrodynamic calculations

The heteronuclear NMR relaxation of globular proteins depends on the anisot ropic rotational diffusion tensor. Using our previous developments for pred iction of hydrodynamic properties of arbitrarily shaped particles, by means of bead models, we have constructed a computational procedure to calculate the rotational diffusion tensor and other properties of proteins from thei r detailed, atomic-level structure. From the atomic coordinates file used t o build the bead model, the orientation of the pertinent dipoles can be ext racted and combined with the hydrodynamic information to predict, for each residue in the protein, the relaxation times. All of these developments hav e been implemented in a computer program, HYDRONMR, which will be of public domain. (C) 2000 Academic Press.