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‐αCH 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. Copyright © 1993, Wiley Blackwell. All rights reserved ; SCOPUS: ar.j ; info:eu-repo/semantics/published