Quantitative Interpretation of Solvent Paramagnetic Relaxation for Probing Protein-Cosolute Interactions.

ABSTRACT: Protein-small cosolute molecule interactions are ubiquitous and known to modulate the solubility, stability, and function of many proteins. Characterization of such transient weak interactions at atomic resolution remains challenging. In this work, we develop a simple and practical NMR method for extracting both energetic and dynamic information on protein-cosolute interactions from solvent paramagnetic relaxation enhancement (sPRE) measurements. Our procedure is based on an approximate (non-Lorentzian) spectral density that behaves exactly at both high and low frequencies. This spectral density contains two parameters, one global related to the translational diffusion coefficient of the paramagnetic cosolute, and the other residue specific. These parameters can be readily determined from

SUBMITTER: Okuno Y 

PROVIDER: S-EPMC7372007 | biostudies-literature | 2020 May

REPOSITORIES: biostudies-literature