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

A. J. Avanov

Institute of Biochemistry, Academy of Sciences of the Armenian SSR, Yerevan

Abstract: Theoretical conformational analysis of C-terminal fragments of tachikinin 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 α-helix with the hydrophobic coat consisted of identically oriented side chains is energetically the most stable structure. The preference of this conformation for tachikinins functioning is discussed.

Russian Journal of Bioorganic Chemistry 1991, 17 (7):937-944

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