Abstract
A protein in solution is a thermodynamic entity, consisting of ensemble of conformers ranging from the lowest-energy folded conformer to the highest-energy unfolded conformer. Under physiological conditions, however, populations of higher energy conformers are small and they are not normally detected by NMR spectroscopy nor by X-ray crystallography. A new type of NMR experiment, utilizing the volume property of a protein in conjunction with pressure, enables structural analysis of semi-stable higher energy conformers, thereby extending the structural analysis essentially to the entire conformational space. The result will provide strong basis for understanding protein function, folding and conformational disease.
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