ZN2+-INDUCED DEPROTONATION OF A PEPTIDE NITROGEN IN ANGIOTENSIN-I
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ARNOLD, AP
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UNIV NEW S WALES COLL,AUSTRALIAN DEF FORCE ACAD,DEPT CHEM,CANBERRA,ACT 2600,AUSTRALIAUNIV NEW S WALES COLL,AUSTRALIAN DEF FORCE ACAD,DEPT CHEM,CANBERRA,ACT 2600,AUSTRALIA
ARNOLD, AP
[1
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STANLEY, DM
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UNIV NEW S WALES COLL,AUSTRALIAN DEF FORCE ACAD,DEPT CHEM,CANBERRA,ACT 2600,AUSTRALIAUNIV NEW S WALES COLL,AUSTRALIAN DEF FORCE ACAD,DEPT CHEM,CANBERRA,ACT 2600,AUSTRALIA
STANLEY, DM
[1
]
COLLINS, JG
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UNIV NEW S WALES COLL,AUSTRALIAN DEF FORCE ACAD,DEPT CHEM,CANBERRA,ACT 2600,AUSTRALIAUNIV NEW S WALES COLL,AUSTRALIAN DEF FORCE ACAD,DEPT CHEM,CANBERRA,ACT 2600,AUSTRALIA
COLLINS, JG
[1
]
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[1] UNIV NEW S WALES COLL,AUSTRALIAN DEF FORCE ACAD,DEPT CHEM,CANBERRA,ACT 2600,AUSTRALIA
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.