Abstract: | The decapeptides Boc-(Aib-L -Ala)5-OMe and Boc-(Aib-L -Val)5-OMe have been studied by 270-MHz 1H-nmr in CDCl3 and (CD3)2SO solutions. Intramolecular hydrogen-bonded NH groups have been delineated using the temperature and solvent dependence of the NH chemical shifts and differential broadening of the NH resonances, induced by addition of a nitroxide radical. Both peptides have eight solvent-shielded NH groups, suggesting that 310-helical conformations are maintained in the two solvents. In alternating Aib-X sequences, the Aib residues appear to play a dominant role in determining the preferred conformations, overriding the intrinsic stereochemical preferences of the X residues. |