H-1-NMR ANALYSIS OF TURKEY EGG-WHITE LYSOZYME AND COMPARISON WITH HENEGG-WHITE LYSOZYME

The complete main chain and approximately 75% of the side chain H-1-NM R assignments of the 129-residue protein, turkey egg-white lysozyme, a re presented. NOE data, hydrogen-exchange rates, chemical shifts and c oupling constants are reported and are indicative of a structure in so lution that is essentially identical to that of the homologous hen egg -white lysozyme. The NH-alphaCH coupling constants of turkey lysozyme are compared to torsion-angle data from three crystal structures of th e protein and the results are interpreted in terms of crystal-structur e resolution and refinement.