FOLDING OF THE INTERACTION OF HISTONE HI WITH SODIUM N-DODECYL SULPHATE
Authors: not saved
Abstract:
The effects of sodium n-dodecyl sulphate (SDS) on the structure of histone HI has been studied by a combination of e:quilibrium dialysis, U.V. spectroscopy ; polyacrylamide gel electrophoresis, protein titration and viscometery techniques using, 2.5 mM phosphate buffer, pH 6.4. The interaction of H, and SDS in contrast tomanyothel-protein-SDS interactions is organized between V 40 to 70. Above V=40 there is an exothermic contribution from HI folding characterized by minima in the enthalpy curve at about 65 Kj mol:' This subject has been confirmed by spectroscopy, electrophoresis , titrametery and viscometery techniques
similar resources
folding of the interaction of histone hi with sodium n-dodecyl sulphate
the effects of sodium n-dodecyl sulphate (sds) on the structure of histone hi has been studied by a combination of e:quilibrium dialysis, u.v. spectroscopy ; polyacrylamide gel electrophoresis, protein titration and viscometery techniques using, 2.5 mm phosphate buffer, ph 6.4. the interaction of h, and sds in contrast tomanyothel-protein-sds interactions is organized between v 40 to 70. above ...
full textThe Unexpected Effect of Sodium Arsenate on the Interaction between Histone H1 and Sodium N-Dodecyl Sulphate
A Study was made on the interaction between histon H1 and sodium n-dodecyl sulphate (SDS) in the presence of sodium arsenate inside a phosphate buffer of pH 6.4, using spectroscopy and equilibrium dialysis at 27 °C. The binding data has been used to obtain the gibbs free energy in terms of a theoretical model based on the Wyman binding potential. The binding data hs been analysed...
full textTHERMODYNAMIC STUDIES OF THE INTERACTION OF SODIUM N-DODECYL, SULPHATE WITH CALF - THYMUS WISTONE H3
The binding of Sodium n-dodecyl sulphate (SDS) to histone H3 was studied in the pH range 3.2-10 by equilibrium dialysis at 27? and 3 7 ?c .T he binding data have been used to obtain the Gibbs free energy of interaction using a theoretical model of the Wyman binding potential; and the enthalpy of interaction from the temperature dependence of theequilibriumconstantsfronr theVan't Hoff re1ati...
full textthe unexpected effect of sodium arsenate on the interaction between histone h1 and sodium n-dodecyl sulphate
a study was made on the interaction between histon h1 and sodium n-dodecyl sulphate (sds) in the presence of sodium arsenate inside a phosphate buffer of ph 6.4, using spectroscopy and equilibrium dialysis at 27 °c. the binding data has been used to obtain the gibbs free energy in terms of a theoretical model based on the wyman binding potential. the binding data hs been analysed in terms of hi...
full textInteraction Studies of Sodium N-Dodecyl Sulphate and Protons to Nistone H1
The relationship between the binding of sodium n-dodecyl sulphate and protons to histone H1 has been investigated by equilibrium dialysis and titrimetry. The data cover the pH range 3.2-10 and surfactant concentrations up to 3.0×10-3 mol dm-3. A theoretical approach based on the binding potential concept of Wyman is presented and has been used to make estima...
full textthermodynamic studies of the interaction of sodium n-dodecyl, sulphate with calf - thymus wistone h3
the binding of sodium n-dodecyl sulphate (sds) to histone h3 was studied in the ph range 3.2-10 by equilibrium dialysis at 27? and 3 7 ?c .t he binding data have been used to obtain the gibbs free energy of interaction using a theoretical model of the wyman binding potential; and the enthalpy of interaction from the temperature dependence of theequilibriumconstantsfronr thevan't hoff re1at...
full textMy Resources
Journal title
volume 1 issue 2
pages -
publication date 1990-03-01
By following a journal you will be notified via email when a new issue of this journal is published.
Hosted on Doprax cloud platform doprax.com
copyright © 2015-2023