Protein conformational changes induced by guanidine at predenaturational concentrations
- 1 November 1988
- journal article
- research article
- Published by Wiley in International Journal of Peptide and Protein Research
- Vol. 32 (5) , 321-325
- https://doi.org/10.1111/j.1399-3011.1988.tb01266.x
Abstract
The nature of the molecular events 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 these observed for liver alcohol dehydrogenase. From the 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.Keywords
This publication has 24 references indexed in Scilit:
- Dynamic aspects of the heme-binding site in phylogenetically distant myoglobinsBiochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology, 1987
- Unfolding pathway of myoglobin: effect of denaturants on solvent accessibility to tyrosyl residues detected by second-derivative spectroscopyBiochemistry, 1987
- Dipolar relaxations in glycerol: a dynamic fluorescence study of 4-[2'-(dimethylamino)-6'-naphthoyl]cyclohexanecarboxylic acid (DANCA)Journal of the American Chemical Society, 1987
- Effects of urea and guanidine hydrochloride on the activity and the dynamical structure of equine liver alcohol dehydrogenaseBiochemistry, 1986
- Myoglobin structure and regulation of solvent accessibility of heme pocketInternational Journal of Peptide and Protein Research, 1985
- Unfolding pathway of myoglobin. Evidence for a multistate processBiochemistry, 1983
- Heme and cysteine microenvironments of tuna apomyoglobin. Evidence of two independent unfolding regionsBiochemistry, 1982
- Nucleation, Rapid Folding, and Globular Intrachain Regions in ProteinsProceedings of the National Academy of Sciences, 1973
- The interaction of a naphthalene dye with apomyoglobin and apohemoglobinJournal of Molecular Biology, 1965
- Cleavage of the haem-protein link by acid methylethylketoneBiochimica et Biophysica Acta, 1959