Angiotensin as a model for hormone – receptor interactions

1985 ◽  
Vol 5 (5) ◽  
pp. 407-416 ◽  
Author(s):  
Graham J. Moore ◽  
John M. Matsoukas

Proton magnetic resonance and chemical reactivity studies have demonstrated the presence of a tyrosine charge relay system in angiotensin which is analogous to the serine charge relay system present at the active site of serine proteases. Receptor activation by angiotensin can be explained by electronic effects deriving from an interaction of the charge relay system with stacking of the histidine and phenylalanine rings. Experiments with serine protease inhibitors suggest the possibility that mechanistic features of the interaction of angiotensin with its receptors may apply to other ‘phenoxyl’ hormones including certain peptides, steroids and catecholamines.

1964 ◽  
Vol 17 (9) ◽  
pp. 967 ◽  
Author(s):  
PR Wells

The proton magnetic resonance spectra of several methylnitronaphthalenes, p-nitrotoluene, and nitro-p-xylene have been determined for dilute carbon tetra- chloride solution. The nitro group has little effect upon the chemical shift of the methyl group unless they are "ortho" related. The electronic effects of the nitro group lead to a general low field shift of the ring protons with little distinction between quinonoid and non-quinonoid positions. From the effect of nitro group rotation due to steric hindrance its anisotropic contribution has been estimated in good agreement with other work.


Sign in / Sign up

Export Citation Format

Share Document