Signal transduction, an important mechanism in a variety of cellular processes (e.g. protein biosynthesis, hormone stimulated metabolic activities, muscle contraction, etc.), is carried out in part through protein conformational changes induced by nucleoside triphosphate binding and hydrolysis. The Fe protein in nitrogenase is one member of this class of proteins. Although structures exist for nitrogenase component proteins, the factors affecting conformational change and MgATP hydrolysis are not well understood. The major objectives of this proposal are to use biochemical, biophysical, and computational techniques (x- ray crystallography, small angle x-ray scattering, calorimetry, and QM/MM calculations) to define conformational changes in the Fe protein during nucleotide binding, hydrolysis, and signal transduction as well as effects of amino acid environment on modulating [4Fe-4S] cluster properties. ? ? ?

Agency
National Institute of Health (NIH)
Institute
National Institute of General Medical Sciences (NIGMS)
Type
Postdoctoral Individual National Research Service Award (F32)
Project #
5F32GM078912-02
Application #
7480328
Study Section
Special Emphasis Panel (ZRG1-F04B-A (20))
Program Officer
Fabian, Miles
Project Start
2007-08-01
Project End
2009-07-31
Budget Start
2008-08-01
Budget End
2009-07-31
Support Year
2
Fiscal Year
2008
Total Cost
$46,826
Indirect Cost
Name
Montana State University - Bozeman
Department
Chemistry
Type
Schools of Arts and Sciences
DUNS #
625447982
City
Bozeman
State
MT
Country
United States
Zip Code
59717