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1: Eur J Biochem. 1993 Jul 15;215(2):255-66.Click here to read Links

1H-NMR analysis of turkey egg-white lysozyme and comparison with hen egg-white lysozyme.

Bartik K, Dobson CM, Redfield C.

Chimie Organique E. P., Université Libre de Bruxelles, Belgium.

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.

PMID: 8344294 [PubMed - indexed for MEDLINE]