SANS STUDIES ON THE BOVINE SERUM ALBUMIN DENATURATION IN THE PRESENCE OF SDS

The effect of the presence sodium dodecyl sulfate (SDS) on denaturation bovine serum albumin (BSA) has been studied using 36 m small-angle neutron scattering (SANS) BATAN spectrometer (SMARTer). data reduction used Graphical Reduction and Analysis SANS Program (GRASP) software, fitting process IGOR software. was identified by observing changes BSA globular structure. experimental results showed addition SDS at low concentrations (2 mM, 5 10 mM) into solution pH 7 do not cause a significant change in size profile fitted with triaxial ellipsoid model, simple shape approach for protein result semi-axis B 2 mM were 33.8 Å, 37.8 respectively. While A C constant those three variations 14.6 Å 32.2 In higher SDS, structure unfolded flexible cylinder radius 14.4 length 83.5 Å. clearly 40 SDS. this condition to fractal dimension 1.1, block 16.7 correlation 42.5 These indicated that caused BSA. Meanwhile, high made unfold lead