Determination of Leu Side-Chain Conformations in Excited Protein States by NMR Relaxation Dispersion

摘要

Protein function is often predicated on the interconversion between highly populated, ground state conformers and low-populated, excited state structures. These excited states are 'invisible' to most of the traditional tools of structural biology but they can be characterized by the Carr- Purcell-Meiboom-Gill (CPMG) relaxation dispersion NMR experiment, so long as their lifetimes are between 0.5 and 10 ms and their population (p_E) exceeds 0.5%.