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
)