Protein structural changes characterized by high-pressure, pulsed field gradient diffusion NMR spectroscopy.

ABSTRACT: Pulsed-field gradient NMR spectroscopy is widely used to measure the translational diffusion and hydrodynamic radius (R_h) of biomolecules in solution. For unfolded proteins, the R_h provides a sensitive reporter on the ensemble-averaged conformation and the extent of polypeptide chain expansion as a function of added denaturant. Hydrostatic pressure is a convenient and reversible alternative to chemical denaturants for the study of protein folding, and enables NMR measurements to be performed on a single sample. While the impact of pressure on the viscosity of water is well known, and our water diffusivity measurements agree closely with theoretical expectations, we find that elevated pressures increase the R_h of dioxane and other small molecules by amounts

SUBMITTER: Ramanujam V 

PROVIDER: S-EPMC7153785 | biostudies-literature | 2020 Mar

REPOSITORIES: biostudies-literature