Britt Thomas of the University of Wyoming is supported by the Experimental Physical Chemistry Program to investigate phospholipid tubule self-assembly and phospholipid membrane-protein interactions using X-ray scattering techniques. The self-assembly studies will explore the roles played by molecular tilt, twist, conformation, and chirality in tubule formation. A comparative study of various genetically-engineered, membrane-bound proteins will extend the X-ray diffraction techniques used to elucidate characteristics of these more complex systems. The education plan of this CAREER award involves the creation of an interdisciplinary teaching program, in which two complementary upper level courses are developed and added to the Chemistry and Molecular Biology Department curricula. The hallmark of nearly all technologically useful biomaterials is the self-assembly of highly-ordered supramolecular structures from simpler components. Phospholipid membrane structures serve as the stage upon which some of the most important processes of life occur, including many catalytic reactions, protein production and folding, and photosynthesis. Results from this study will be used to improve the understanding of lipid membrane properties, and could subsequently impact the technological development of membrane-based optical switches, molecular electronics, molecular sieves, and chemical/biological sensors. The educational component of this award will encourage collaboration among students and faculty in two separate academic departments at the University of Wyoming, by enhancing cross-disciplinary teaching and research efforts.

Agency
National Science Foundation (NSF)
Institute
Division of Chemistry (CHE)
Type
Standard Grant (Standard)
Application #
9734266
Program Officer
Janice M. Hicks
Project Start
Project End
Budget Start
1998-06-01
Budget End
2000-10-31
Support Year
Fiscal Year
1997
Total Cost
$358,501
Indirect Cost
Name
University of Wyoming
Department
Type
DUNS #
City
Laramie
State
WY
Country
United States
Zip Code
82071