The Structural States of Ion Channel Proteins in Solution and Bound to Lipid Vesicles


Elaine R. Chan1, John J. Kasianowicz1, Kenneth A. Rubinson1, Susan Krueger2


1Semiconductor Electronics Division, Electronics and Electrical Engineering Laboratory

2NIST Center for Neutron Research



            Neutron scattering is a powerful technique for probing the structural properties of molecules at atomic and nanometer length scales.  We are conducting small-angle neutron scattering (SANS) measurements of the transmembrane protein alpha-hemolysin under physiologically relevant conditions to determine its structural properties when it is in solution and bound to lipid vesicles.  SANS measurements of the protein in different structural states will be presented.  We deduce information on transmembrane channel structure from the scattering data after determining the contrast match points of the deuterated lipid vesicles in solution.  The utility of SANS in transmembrane protein structural determination should enable further insights on the roles of these sophisticated structures in cell regulatory pathways and infection and disease.



Speaker: Elaine R. Chan

Mentor: John J. Kasianowicz

Semiconductor Electronics Division

Electronics and Electrical Engineering Laboratory

Bldg. 225/Room A305

Mail Stop 8120

Tel: (301) 975-5787

Fax: (301) 975-5668


Sigma Xi member: No


Category: Biology