par Bartik, Kristin ;Dobson, C M;Redfield, Christina
Référence European journal of biochemistry / FEBS, 215, 2, page (255-266)
Publication Publié, 1993-07
Article révisé par les pairs
Résumé : The complete main chain and approximately 75% of the side chain 1H-NMR assignments of the 129-residue protein, turkey egg-white lysozyme, are presented. NOE data, hydrogen-exchange rates, chemical shifts and coupling constants are reported and are indicative of a structure in solution that is essentially identical to that of the homologous hen egg-white lysozyme. The NH-alpha CH coupling constants of turkey lysozyme are compared to torsion-angle data from three crystal structures of the protein and the results are interpreted in terms of crystal-structure resolution and refinement.