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A computergraphic determination of the chemotactic peptide preferred conformation.

Abstract：

:Replacement of leucine in the chemotactic peptide For-Met-Leu-Phe by the sterically constrained amino acids alpha-aminoisobutyric acid and aminocyclohexanecarboxylic acid affords compounds of equal or greater activity than the parent. NMR studies indicate that the parent compound is present as a beta-sheet in solution, whereas the analogues prefer a beta-turn. Application of molecular modelling would indicate that the beta-turn conformer is energetically preferable and thus suggests that it is the orientation adopted by the peptides.

journal_name

Biochem Biophys Res Commun

journal_title

Biochemical and biophysical research communications

authors

Semus SF,Becker EL,Toniolo C,Freer RJ

doi

10.1016/s0006-291x(88)80287-0

subject

Has Abstract

pub_date

1988-12-15 00:00:00

pages

569-74

issue

2

eissn

0006-291X

issn

1090-2104

pii

S0006-291X(88)80287-0

journal_volume

157

pub_type

杂志文章

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