Dynamics in Polypeptides by Solid State 2H NMR

Abstract

A review. Solid state 2H NMR parameters are almost exclusively governed by the quadrupole interaction with elec. field gradient (EFG) tensor at the deuteron site. The EFG is entirely intramol. in nature. Thus, mol. order and mobility are monitored through the orientation of individual C-2H bond direction. Therefore, 2H NMR is a powerful technique for studying local mol. motions. It enables one to discriminate different types of motions and its correlation times over the wide frequency range. The side chains of a polypeptide have remarkable multiple motional freedom about multiple bonds, while the main chain forms regular secondary conformation such as .alpha.-helix and .beta.-sheet which are presumed to be a rigid structure. In this section, we focus on the dynamics of both side- and main-chains of synthetic polypeptides deuterated at several positions by solid state 2H NMR.Editor(s): Webb, Graham A. Publisher: Springer, Dordrecht, Neth