1H-NMR analysis of turkey egg-white lysozyme and comparison with hen egg-white lysozyme.
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.
Bartik
K
K
Chimie Organique E. P., Université Libre de Bruxelles, Belgium.
Dobson
C M
CM
Redfield
C
C
D000595:Amino Acid Sequence; D000818:Animals; D002645:Chickens; D004529:Egg White; D009682:Magnetic Resonance Spectroscopy; D008969:Molecular Sequence Data; D009113:Muramidase / Q000737:chemistry*; D014421:Turkey; D014961:X-Ray Diffraction
D009113:Muramidase