Complex role of solvation in protein structure and dynamics in micelles and membranes

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One of the great challenges in biological chemistry is to develop a fundamental understanding of how protein structure informs function. By encapsulating proteins in surfactant micelles (nanoscale molecular aggregates, such as a droplet in a colloidal system), experimental studies have shown that critical insights can be gained into protein structure, dynamics, and function. Currently, however, no one knows how the micelle environment influences the structure and dynamics of the encapsulated proteins. In this project, funded by the Chemical Theory, Models and Computational Methods Program of the Chemistry Division, Professor John Straub of Boston University leads a computational study to develop a fundamental understanding of the nature and potential applications of protein encapsulation in micelles.The project involves a systematic computational study of the effect of varying surfactant properties on the structure and dynamics of micelle encapsulated proteins. Through a novel multiscale computational approach, the influence of surfactant (anionic, cationic, and mixtures) and relative impact of generic (confinement geometry, spatially-dependent pressure profile) and surfactant specific contributions, on properties such as association equilibria, hydration dynamics, and channel function, will be explored. Novel and traditional approaches will be employed to analyze structure, dynamics, and function for comparison with observables from NMR and vibrational spectroscopy. The broader impact of the study is the promotion of graduate education in computational biophysics through the development of a summer school for graduate training in state-of-the-art computational and experimental methods in the field of biomolecular structure and dynamics. Participating students will be selected to provide a balance of experimentalists and theorists, women and men, with a strong involvement of underrepresented minorities.