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 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