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.

引用

页码：255 / 266

页数：12

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