The immunoglobulin-binding B1 domain of Streptococcal Protein G (GB1) is often used as a model to understand protein stability, folding,<br/>and dynamics. The conformational motion of GB1 is known to change drastically when the protein is subjected to specific point mutations. Here, data from 77Se NMR spectroscopy and molecular dynamics (MD) simulations are combined to characterize the effects of selenomethionine substitutions in GB1. Importantly, all-atom MD simulations can reveal fine details of protein motion that are inaccessible to experiments, much like a computational microscope. Owing to GB1’s relatively small size, it is also used here as a model for developing approaches to make the computational microscope accessible to individuals who are visually-impaired.

Effects of selenomethionine substitutions on the GB1 model protein characterized by all-atom molecular dynamics simulations

Macromolecular Chemistry: The Second Century

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ACS Spring 2020 National Meeting & Expo

The official archive and repository for all ACS Meetings & Expositions abstracts and select posters or presentations.