PROTON MAGNETIC RESONANCE STUDIES OF HUMAN LYSOZYME

被引:48
作者
COHEN, JS
机构
[1] Department of Biophysics and Pharmacology, Merck Institute for Therapeutic Research, Rahway
关键词
D O I
10.1038/223043a0
中图分类号
O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];
学科分类号
07 ; 0710 ; 09 ;
摘要
The high pK value of the single histidine residue of human lysozyme (7.1 at 32°C), together with thermodynamic data, indicate that this histidine is in a negatively charged environment and is partially buried. The histidine residue is not at the binding site for oligosaccharide inhibitors. Highly shielded tryptophan residues are at the binding site and are involved identically in the binding of both di and tri-N-acetylglucosamine. © 1969 Nature Publishing Group.
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页码:43 / +
页数:1
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