Studies of Polypeptide Structure by Fluorescence Techniques
Year: 1966
Type: article
Abstract: Changes in temperature and in viscosity affect dye-poly Glu63Lys37 (No. 3) conjugates in different ways. Variation of temperature in solutions of different initial viscosities (up to 9 centipoise at 10°) shows a constant transition temperature (10°) for the polypeptide above which there is accelerated depolarization; at higher viscosities no such thermal transition occurs. In contrast, the transition to accelerated depolarization cannot be induced by changes of viscosity alone. Changes in viscosity at a series of constant temperatures show separate effects due to the dye moiety and to the polypeptide chain. The plot of (1/p + 1/3) against 1/e shows two distinct relaxation times for the 1-dimethylaminonaphthalenesulfonyl-labeled polymer, and for the fluorescein-labeled polymer it shows a series of straight lines, each of which has a different slope and a slight deviation concave to the 1/e axis at high viscosities. The rotational relaxation time of the polypeptide conjugated with 1-dimethylaminonaphthalenesulfonyl chloride is twice that measured with the fluorescein conjugate in aqueous solution, but not in glycerol solutions.
Source: Journal of Biological Chemistry
Authors: Gilbert S. Omenn, Thomas J. Gill
Institution: Harvard University
Language: English
Subfield: Molecular Biology
Domain: Life Sciences
Open Access status: hybrid
Estimated APC paid: $3,430
OpenAlex ID: W1496388670