Coupling between protein, water, and protonation dynamics in channelrhodopsins and photosystem II (C04)

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Functionally crucial processes in channelrhodopsin-2 (ChR2) and photosystem II (PSII) involve changes in the protonation states of specific amino acid residues of the protein. The key open question of how changes in protonation couple with both protein conformational dynamics and water dynamics is addressed. Theoretical biophysics techniques are used to study the dynamics of ChRs and PSII in hydrated lipid membrane environments, probe the response of protein and water dynamics to changes in protonation or mutations, dissect hydrogen-bonded networks and compute proton-transfer pathways.