Berlin 2015 – wissenschaftliches Programm

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BP: Fachverband Biologische Physik

BP 17: Posters: Protein structure and dynamics

BP 17.11: Poster

Montag, 16. März 2015, 17:30–19:30, Poster A

Water Dynamics Near Fluorinated Amino Acids: A Molecular Dynamics Study — •João R. Robalo and Ana Vila Verde — Max Planck Institute of Colloids and Interfaces, Potsdam, Germany

Incorporating fluorinated amino acids into proteins often results in increases of protein resistance to thermal and chemical degradation, as well as in improved functionality. Recent work by B. Koksch and co-workers [1] suggests that changes in protein function upon fluorination of amino acids at the protein active site may arise from the different behavior of water near those amino acids, compared to their non-fluorinated analogues. At present, however, the structure and dynamics of water near fluorinated proteins is not understood. We are addressing this issue by developing classical, all-atom, fixed-charge models of fluorinated hydrophobic amino acids and using them to investigate water structure and dynamics in their vicinity. The models are parameterized to reproduce experimental free energies of hydration of fluorinated analogues of hydrophobic amino acid side chains. The developed models shall then be used for the study of water near fluorinated small peptides and proteins.

[1] - B. Koksch, unpublished