CONFORMATIONAL CHARACTERIZATION OF CYCLOPENTAPEPTIDE, LVAL‐LPRO‐GLY‐LVAL‐GLY: A REPEATING ANALOGUE OF ELASTIN

Academic Article

Abstract

  • The cyclopentapeptide, ·L·Val1‐L· Pro2‐Gly3‐L· Val4‐Gly5, was synthesized and its conformational characterization was carried out using n.m.r. and theoretical energy calculations. The n.m.r. studies indicated the existence of a cis Val1‐Pro2 peptide bond in water and a very strong intramolecular H‐bond between the Val1 NH and Gly3 C=O groups. This H‐bond forms a β‐turn (type II) placing Val4 Gly5 residues within the turn. Two minimum energy conformations were derived, one of which agrees very well with the solution conformation. © 1981 Munksgaard, Copenhagen
  • Authors

    Digital Object Identifier (doi)

    Author List

  • KHALED MA; VENKATACHALAM CM; SUGANO H; URRY DW
  • Start Page

  • 23
  • End Page

  • 33
  • Volume

  • 17
  • Issue

  • 1