Loop mobility in proteins has been associated with many fundamental properties<br/>such as catalysis, gating, ligands access, etc.. Conformational changes of loops can be triggered by many events. In several lipocalin a loop at the entrance of the<br/>internal pocket appears to be triggered by an unusual protonation/deprotonation of<br/>an acidic residue. In bovine beta-lactoglobulin (BLG) this residue is a Glu at position<br/>89 position at the beginning of a loop (EF loop). A survey of available BLG structures reveals that the side chain of Glu 89 is parallel to the opening of the internal pocket but in some structures, the protonatable amino group is under the loop while in others is on the outside of the loop. We have tested this event using 200 ns all atoms molecular dynamic simulations. We have demonstrated that only in structures where the Glu side chain is directly under the EF loop, the deprotonation of the residue prompts a conformational transition of the loop. These changes were not previously detected by MD simulations.

All atom 200-ns simulations of loop transitions in a lipocalin

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.