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
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
收藏
页码:96 / 98
页数:3
相关论文
共 13 条