Protein conformational changes induced by guanidine at predenaturational concentrations.
The nature of the molecular event that apomyoglobin undergoes at predenaturational concentrations of guanidine has been investigated by means of steady-state and multifrequency phase and modulation fluorometry. The results have been compared to those observed for liver alcohol dehydrogenase. From these studies has been hypothesized a different susceptibility of the distinct elements of secondary, super-secondary, and tertiary structure towards the denaturing action of guanidine at predenaturational concentrations.
Bismuto
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E
Section for Chemistry and Biochemistry, Faculty of Medicine, University of Naples, Italy.
Irace
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G
D000426:Alcohol Dehydrogenase; D001059:Apoproteins / Q000378:metabolism; D005456:Fluorescent Dyes; D019791:Guanidine; D006146:Guanidines / Q000494:pharmacology*; D008099:Liver / Q000201:enzymology; D009211:Myoglobin / Q000378:metabolism; D009282:Naphthalenesulfonates / Q000378:metabolism; D011489:Protein Denaturation / Q000187:drug effects*; D013050:Spectrometry, Fluorescence
D001059:Apoproteins; D005456:Fluorescent Dyes; D006146:Guanidines; D009211:Myoglobin; D009282:Naphthalenesulfonates; C010857:apomyoglobin; C009497:2-(4-toluidino)-6-naphthalenesulfonic acid; D000426:Alcohol Dehydrogenase; D019791:Guanidine