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Conformational analysis of tachykinins. III. C-terminal fragment Asx-Xaa-Phe-Yaa-Gly-Leu-Met-NH2

Avanov, A.I.

Bioorganicheskaia Khimiia 17(7): 937-944

1991

ISSN/ISBN: 0132-3423
PMID: 1793435
Document Number: 376876
Theoretical conformational analysis of C-terminal fragments of tachykinin peptides with a common amino acid sequence Asx-Xaa-Phe-Yaa-Gly-Leu-Met-NH2 suggested the conformational states to be independent of the nature of Xaa and Yaa residues. It is shown that among plausible spatial forms of the C-terminal fragments an alpha-helix with the hydrophobic coat consisted of identically oriented side chains is energetically the most stable structure. The preference of this conformation for tachykinins functioning is discussed.

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