COLLECTIVE NMR RELAXATION MODEL APPLIED TO PROTEIN DYNAMICS

A new dynamical model for the interpretation of nuclear magnetic reson ance relaxation data is presented. It is based on a normal mode descri ption, treating the low frequencies associated with collective motions as adjustable parameters to optimize agreement between calculated and experimental relaxation order parameters. This model provides a compa ct representation of many aspects of internal dynamics and characteriz es motions affecting different spin pairs in a correlated way. Further more, it links together dynamical characteristics of different types o f NMR observables and allows one to assess vibrational thermodynamic p roperties. Sample applications are given for a 25-residue zinc-finger peptide.