Simultaneously measured low temperature absorption and circular dichroic spectra are presented for different intermediates of the bacteriorhodopsin photocycle in suspension and hydrated film of purple membranes. The data for the L intermediate are in accord with excitonic interpretation of the visible part of the circular dichroic spectrum, suggesting that no large scale structural change of the purple membrane affecting its crystalline structure happens during the L formation. The structure of the membrane, which is disrupted in the M state, is recovered when M is illuminated with blue light at low temperature.
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