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Can Retinal Isomerization in Bacteriorhodopsin Be Coherently Controlled in the Strong Field Limit?

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Abstract

We observe experimentally that the isomerization efficiency of bacteriorhodopsin increases by chirping the excitation pulses at moderate excitation levels. Under strong fields (>100 GW/cm2), the isomerization becomes corrupted, most likely from ionization of the protein.

© 2010 Optical Society of America

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