We present the results of a comparative study of the binding of carbon monoxide to myoglobin in glycerol/buffer solution with different concentrations of guanidine hydrochloride, under extended illumination over the temperature range 30-80 K. The changes in the Sorer band indicate that the folding state of the protein is a key parameter in determining the photodissociation process and the relaxation rate of the protein.
Light induced states in MbCO denatured with guanidine hydrochloride
DELLA LONGA, STEFANO;
1998-01-01
Abstract
We present the results of a comparative study of the binding of carbon monoxide to myoglobin in glycerol/buffer solution with different concentrations of guanidine hydrochloride, under extended illumination over the temperature range 30-80 K. The changes in the Sorer band indicate that the folding state of the protein is a key parameter in determining the photodissociation process and the relaxation rate of the protein.File in questo prodotto:
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