This is a shared instrumentation request to replace an ailing 22-year old instrument with state-of-the-art capabilities. The high, highly active Core Group faculty have projects covering: calcium binding proteins which fold via the molten globule; preparation and utilization of various myoglobin and carbonic anhydrase mutants and forms to be probed by electron spin resonance methods for intramolecular distance measurements in solution; kinetics and mechanism of folding of a variety of proteins, enzymes and their mutants; and detailed investigations of denatured state energetics. There is a strong institutional emphasis on research as reflected by a 20% cost-sharing commitment and guarantees of maintenance and operating costs throughout the period of this project and beyond. This is a relatively small funding request to the NIH which will certainly be 'value-added' in the ability to generate new and important research from both the NIH funded grantees as well as other user groups generating meaningful results for planning future NIH, federal and other funded research programs. Lastly, as additional 'value- added,' the involvement of collaborative NIH supported researchers at the University of Colorado Health Sciences Center underscores the shared nature of this instrumentation that reaches out beyond the sponsoring institution.

Agency
National Institute of Health (NIH)
Institute
National Center for Research Resources (NCRR)
Type
Biomedical Research Support Shared Instrumentation Grants (S10)
Project #
1S10RR016632-01
Application #
6439366
Study Section
Special Emphasis Panel (ZRG1-PB (01))
Program Officer
Tingle, Marjorie
Project Start
2002-05-01
Project End
2003-04-30
Budget Start
2002-05-01
Budget End
2003-04-30
Support Year
1
Fiscal Year
2002
Total Cost
$116,146
Indirect Cost
Name
University of Denver
Department
Chemistry
Type
Schools of Arts and Sciences
DUNS #
City
Denver
State
CO
Country
United States
Zip Code
80208
Baddam, Saritha; Bowler, Bruce E (2006) Mutation of asparagine 52 to glycine promotes the alkaline form of iso-1-cytochrome c and causes loss of cooperativity in acid unfolding. Biochemistry 45:4611-9
Baddam, Saritha; Bowler, Bruce E (2006) Tuning the rate and pH accessibility of a conformational electron transfer gate. Inorg Chem 45:6338-46
Redzic, Jasmina S; Bowler, Bruce E (2005) Role of hydrogen bond networks and dynamics in positive and negative cooperative stabilization of a protein. Biochemistry 44:2900-8
Kristinsson, Richard; Bowler, Bruce E (2005) Communication of stabilizing energy between substructures of a protein. Biochemistry 44:2349-59
Baddam, Saritha; Bowler, Bruce E (2005) Thermodynamics and kinetics of formation of the alkaline state of a Lys 79-->Ala/Lys 73-->His variant of iso-1-cytochrome c. Biochemistry 44:14956-68
Martinez, Robert E; Bowler, Bruce E (2004) Proton-mediated dynamics of the alkaline conformational transition of yeast iso-1-cytochrome c. J Am Chem Soc 126:6751-8
Wandschneider, Eydiejo; Hammack, Barbara N; Bowler, Bruce E (2003) Evaluation of cooperative interactions between substructures of iso-1-cytochrome c using double mutant cycles. Biochemistry 42:10659-66