Abstract
Inhomogeneous broadening of visual pigment spectra may be due, in part, to the known dynamic conformational properties of protein molecules. As a consequence, the blue-shifted species formed by long-wavelength irradiation of rhodopsin at very low temperatures could be an artefact arising from photoselection (“hole burning”) of different conformational substates of the protein chromophore in the frozen matrix. Numerical simulation of this process mimics many of the observed spectral properties of hypsorhodopsin.
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