Analysis of Fluctuating Protein Structure

- Approach from Variable Pressure NMR

Abstract

Protein structure in solution fluctuates over a wide range of conformation, but the reality of the fluctuation has been little explored. In this article, we present an approach to this problem using variable pressure NMR spectroscopy. The method enables us to explore protein conformation over a wide range of conformational space than hitherto explored by conventional NMR method and brings about a new dynamic view on protein structure. The highlight of the method is the determination of the structural coordinates of semi-stable higher energy conformers that exist in low population in dynamic equilibrium with the stable "native" conformer under physiological conditions. Available evidence suggests that such high energy conformers play crucial roles in function in many proteins.