[Conformational analysis of tachykinins. III. C-terminal fragment Asx-Xaa-Phe-Yaa-Gly-Leu-Met-NH2].
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.
Avanov
A Ia
AIa
D000595:Amino Acid Sequence; D008969:Molecular Sequence Data; D011487:Protein Conformation; D013329:Structure-Activity Relationship; D015320:Tachykinins / Q000737:chemistry*
D015320:Tachykinins
Konformatsionnyĭ analiz takhikininov. III. C-kontsevoĭ fragment Asx-Xaa-Phe-Yaa-Gly-Leu-Met-NH2.