ZN2+-INDUCED DEPROTONATION OF A PEPTIDE NITROGEN IN ANGIOTENSIN-I

被引：10

作者：

ARNOLD, AP ^{[1
]}

STANLEY, DM ^{[1
]}

COLLINS, JG ^{[1
]}

机构：

[1] UNIV NEW S WALES COLL,AUSTRALIAN DEF FORCE ACAD,DEPT CHEM,CANBERRA,ACT 2600,AUSTRALIA

来源：

FEBS LETTERS | 1991年 / 289卷 / 01期

关键词：

H-1-NMR; ZINC BINDING; DEPROTONATED AMIDE; ANGIOTENSIN-I; PEPTIDE;

D O I：

10.1016/0014-5793(91)80916-Q

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 interaction of Zn2- with angiotensin I, a decapeptide containing two histidyl residues, has been studied by H-1-NMR spectroscopy in both water and dimethylsulfoxide. When Zn2- is added to the peptide in dimethylsulfoxide, binding occurs by coordination of the imidazole rings of both histidines to the metal-ion, enabling the deprotonation of the Phe peptide nitrogen.

引用

页码：96 / 98

页数：3

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