Most thiol oxidoreductases contain the well conserved thioredoxin fold. This fold is present in both oxidasesand disulfide reductases. I intend to address how can different members of the thioredoxin family thoughthey all have the same fold differ so greatly in their chemistry and reactivity. I will force thiol thiol reductasesinto thiol oxidases by selecting for mutants that are able to complement a thiol oxidase deficiency. Theresults garnered from this work will allow us to investigate how structure and function are related andhow.Diseases such as sickle cell anemia and cystic fibrosis are caused by small mutations in a general fold thatrenders the protein inactive. Our work will investigate how small mutational changes can affectdirectionality of a reaction, which will help elucidate how small mutations within normal proteins can causethem to become diseased.

Agency
National Institute of Health (NIH)
Institute
National Institute of General Medical Sciences (NIGMS)
Type
Predoctoral Individual National Research Service Award (F31)
Project #
5F31GM077084-02
Application #
7171850
Study Section
Special Emphasis Panel (ZRG1-GGG-G (29))
Program Officer
Toliver, Adolphus
Project Start
2006-01-01
Project End
2007-01-31
Budget Start
2007-01-01
Budget End
2007-01-31
Support Year
2
Fiscal Year
2007
Total Cost
$10,214
Indirect Cost
Name
University of Michigan Ann Arbor
Department
Biochemistry
Type
Schools of Arts and Sciences
DUNS #
073133571
City
Ann Arbor
State
MI
Country
United States
Zip Code
48109
Catapano, Joshua Stephen; John Hawryluk, Gregory William; Whetstone, William et al. (2016) Higher Mean Arterial Pressure Values Correlate with Neurologic Improvement in Patients with Initially Complete Spinal Cord Injuries. World Neurosurg 96:72-79