Bioactive peptides: conformational studies of [Tyr4] cyclolinopeptide A.

Abstract:

:The solid state conformational analysis of [Tyr4] cyclolinopeptide A has been carried out by x-ray diffraction studies. The crystal structure of the monoclinic form, grown from a dioxane-water mixture [alpha = 9.849 (5) A, b = 20.752 (4) A, c = 16.728 (5) A, beta = 98.83 (3) degrees, space group P21, Z = 2], shows the presence of five intramolecular N-H...O = C hydrogen bonds, with formation of one C17 ring structure, one alpha-turn (C13), one inverse gamma-turn (C7), and two beta-turns (C10, one of type III and one of type I). The Pro1-Pro2 peptide unit is cis (omega = 5 degrees), all others are trans. The structure is almost superimposable with that of cyclolinopeptide A. The rms deviation for the atoms of the backbones is on the average 0.33 A.

journal_name

Biopolymers

journal_title

Biopolymers

authors

Saviano M,Rossi F,Filizola M,Isernia C,Di Blasio B,Benedetti E,Pedone C,Siemion IZ,Pedyczak A

doi

10.1002/bip.360360408

subject

Has Abstract

pub_date

1995-10-01 00:00:00

pages

453-60

issue

4

eissn

0006-3525

issn

1097-0282

journal_volume

36

pub_type

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