Abstract Listing

Listing Use your browser’s Print button, or File-Print command sequence. 530356: Effects of guanidine hydrochloride on the structure and properties of beta-casein in solution and at interface with air PHYS 0 [530356]: Effects of guanidine hydrochloride on the structure and properties of beta-casein in solution and at interface with air Adel Aschi, Departement of Physics, Tunisia University, Laboratoire de Physique de la Matière Molle, Faculté des Sciences de Tunis, Tunis 1060, Tunisia, Fax: + 216 71 885 073, aschi13@yahoo.fr ACCEPTED Topic Selection: Applications of Neutron Scattering in Structural Biology and Biophysics: Structure and association of biomolecules in solution Invited: Y Preferred Presentation Format: OralOnly Consider for Sci-Mix: Y Special Equipment Needs: overhead projector Conforms to Bylaw 6: Y Last Modified: 2002-04-02 Abstract We have examined the small-angle neutron scattering (SANS) profile of beta-casein in the native state and in highly denaturing conditions. It shows that the neutron spectra given by unfolded beta-casein are similar to those of excluded volume polymer chains. Adsorption layers of beta-casein formed from a buffer including various concentrations of guanidine hydrochloride (gdmCl) have been studied by neutron reflectivity. A transition in the structure and in the properties of the adsorption layer seems to occur around a gdmCl concentration of 1.5 M. These data are interpreted assuming that the adsorbed protein molecules behave like multi-block copolymers with alternating hydrophilic and hydrophobic sequences.We have examined the small-angle neutron scattering (SANS) profile of beta-casein in the native state and in highly denaturing conditions. It shows that the neutron spectra given by unfolded beta-casein are similar to those of excluded volume polymer chains. Adsorption layers of beta-casein formed from a buffer including various concentrations of guanidine hydrochloride (gdmCl) have been studied by neutron reflectivity. A transition in the structure and in the properties of the adsorption layer seems to occur around a gdmCl concentration of 1.5 M. These data are interpreted assuming that the adsorbed protein molecules behave like multi-block copolymers with alternating hydrophilic and hydrophobic sequences. 530380: Hydrogen and hydration in proteins PHYS 0 [530380]: Hydrogen and hydration in proteins Nobuo Niimura, Advanced Science Research Center, Japan Atomic Energy Research Institute, Tokai-mura, Naka-gun, Ibaraki-ken 319-1195, Japan, Fax: 81-29-282-5927, niimura@kotai3.tokai.jaeri.go.jp