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Theoretical conformational analysis of Asn 1 , Val 5 angiotensin II
Author(s) -
De Coen JeanLouis,
Ralston Evelyn
Publication year - 1977
Publication title -
biopolymers
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.556
H-Index - 125
eISSN - 1097-0282
pISSN - 0006-3525
DOI - 10.1002/bip.1977.360160908
Subject(s) - chemistry , angiotensin ii , side chain , molecule , proline , crystallography , peptide , stereochemistry , amino acid , biochemistry , organic chemistry , receptor , polymer
A theoretical analysis of the conformation of the octapeptide hormone Asn 1 , Val 5 angiotensin II has been carried out by semiempirical potential energy calculations. A preliminary study of the Ala 6 ‐Pro‐Ala molecule, which mimics the angiotensin backbone, provided us with likely backbone structures on which the effect of the full side chains of the hormone could be assessed. For angiotensin II, the calculations show that only a small number of folded, compact conformations have a high probability of existence. This is the consequence of favorable packing and of the presence of proline in position 7. These results are consistent with various experimental data, both structural and biological. This method is readily applicable to the study of analogs of the hormone or to other peptides of comparable size.