A simple method for measuring signs of (1)H (N) chemical shift differences between ground and excited protein states.

ABSTRACT: NMR relaxation dispersion spectroscopy is a powerful method for studying protein conformational dynamics whereby visible, ground and invisible, excited conformers interconvert on the millisecond time-scale. In addition to providing kinetics and thermodynamics parameters of the exchange process, the CPMG dispersion experiment also allows extraction of the absolute values of the chemical shift differences between interconverting states, /Delta(omega)/, opening the way for structure determination of excited state conformers. Central to the goal of structural analysis is the availability of the chemical shifts of the excited state that can only be obtained once the signs of Delta(omega) are known. Herein we describe a very simple method for determining the signs of (1)H(N) Delta(omega) values

SUBMITTER: Bouvignies G 

PROVIDER: S-EPMC3034452 | biostudies-literature | 2010 Jun

REPOSITORIES: biostudies-literature