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

被引：16
作者：
BARTIK, K
DOBSON, CM
REDFIELD, C
机构：
[1] UNIV OXFORD,INORGAN CHEM LAB,S PARKS RD,OXFORD OX1 3QR,ENGLAND
[2] UNIV OXFORD,OXFORD CTR MOLEC SCI,OXFORD,ENGLAND
[3] UNIV LIBRE BRUXELLES,CHIM ORGAN EP,B-1050 BRUSSELS,BELGIUM
来源：
EUROPEAN JOURNAL OF BIOCHEMISTRY | 1993年 / 215卷 / 02期
关键词：
D O I：
10.1111/j.1432-1033.1993.tb18030.x
中图分类号：
Q5 [生物化学]; Q7 [分子生物学];
学科分类号：
071010 ; 081704 ;
摘要：
The complete main chain and approximately 75% of the side chain H-1-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-alphaCH 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.
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页码：255 / 266
页数：12
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