[Structure-function organization of neurokinin A and neurokinin B molecules. I. Theoretical conformational analysis of neurokinin A].
The spatial structure of the neurokinin A molecule was studied by the method of theoretical conformational analysis. On the basis of fragmental analysis, stable structures of the neurokinin A molecule under polar conditions were determined. The structures can be described by four families of low-energy conformations having a relatively labile tripeptide at the C-end and a conformationally rigid heptapeptide at the N-end. It was shown that two of these conformations are virtually isoenergetic structures. One of these is an alpha-helical structure and the other forms two beta-turns at the N-terminus, which change to the turn of the alpha-helix at the C-end.
Agaeva
G A
GA
Kerimli
N N
NN
Godzhaev
N M
NM
D000595:Amino Acid Sequence; D008958:Models, Molecular; D008969:Molecular Sequence Data; D015288:Neurokinin A / Q000737:chemistry*; D015287:Neurokinin B / Q000737:chemistry; D011487:Protein Conformation
D015288:Neurokinin A; D015287:Neurokinin B