Spatial structures of tripeptides glycylglycyl-l-histidine and glycylglycyl-l-tyrosine based on residual dipolar couplings and quantum-chemical computations

Abstract

A novel approach to the determination of the spatial structure of oligopeptides on the basis of an analysis of the residual dipolar couplings 1H-13C assisted by quantum-chemical computations with considering solvent effects is proposed to characterize the conformations of the tripeptides GlyGlyHis and GlyGlyTyr with significant folding of the latter to left-handed helix. © 2011 Mendeleev Communications. All rights reserved