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.
Titolo: | Light induced states in MbCO denatured with guanidine hydrochloride |
Autori: | |
Data di pubblicazione: | 1998 |
Rivista: | |
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. |
Handle: | http://hdl.handle.net/11697/9717 |
Appare nelle tipologie: | 1.1 Articolo in rivista |
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