6533b86cfe1ef96bd12c8384

RESEARCH PRODUCT

Conformational studies of hexapeptides containing two dehydroamino acid residues in positions 3 and 5 in peptide chain

Artur KrężelRafał LatajkaMichał JewgińskiMaciej Makowski

subject

chemistry.chemical_classificationconformationCircular dichroismStereochemistryHydrogen bondOrganic ChemistryBent molecular geometryCD spectroscopyPeptidedehydroalanineNMRAnalytical ChemistryInorganic Chemistrychemistry.chemical_compoundchemistryChain (algebraic topology)DehydroalanineIntramolecular forceisomers of dehydrophenylalanineConformational isomerismSpectroscopy

description

Abstract Synthesis and structural studies of hexapeptides containing two dehydroamino acid residues in positions 3 and 5 in a peptide chain were performed. All the investigated peptides adopted bent conformations, stabilized by intramolecular hydrogen bonding, and could exist as two different conformers in solution. Only in the case of the peptide containing ΔAla residues, expected 3 10 -helical conformation was found.

yearjournalcountryeditionlanguage
2008-12-01Journal of Molecular Structure
10.1016/j.molstruc.2008.06.023https://www.sciencedirect.com/science/article/pii/S0022286008004559#!