Agency
National Institute of Health (NIH)
Institute
National Institute on Aging (NIA)
Type
Research Project (R01)
Project #
2R01AG009761-06A1
Application #
2051039
Study Section
Molecular and Cellular Biophysics Study Section (BBCA)
Program Officer
Finkelstein, David B
Project Start
1990-09-01
Project End
1998-11-30
Budget Start
1995-12-20
Budget End
1996-11-30
Support Year
6
Fiscal Year
1996
Total Cost
Indirect Cost
Name
University of Michigan Ann Arbor
Department
Other Health Professions
Type
Schools of Medicine
DUNS #
791277940
City
Ann Arbor
State
MI
Country
United States
Zip Code
48109
Fischer, Christopher J; Gafni, Ari; Steel, Duncan G et al. (2002) The triplet-state lifetime of indole in aqueous and viscous environments: significance to the interpretation of room temperature phosphorescence in proteins. J Am Chem Soc 124:10359-66
Dirnbach, E; Steel, D G; Gafni, A (2001) Mg2+ binding to alkaline phosphatase correlates with slow changes in protein lability. Biochemistry 40:11219-26
Fischer, C J; Schauerte, J A; Wisser, K C et al. (2001) Differences in the pathways for unfolding and hydrogen exchange among mutants of Escherichia coli alkaline phosphatase. Biochim Biophys Acta 1545:96-103
Fischer, C J; Schauerte, J A; Wisser, K C et al. (2000) Hydrogen exchange at the core of Escherichia coli alkaline phosphatase studied by room-temperature tryptophan phosphorescence. Biochemistry 39:1455-61
Gershenson, A; Schauerte, J A; Giver, L et al. (2000) Tryptophan phosphorescence study of enzyme flexibility and unfolding in laboratory-evolved thermostable esterases. Biochemistry 39:4658-65
Dirnbach, E; Steel, D G; Gafni, A (1999) Proline isomerization is unlikely to be the cause of slow annealing and reactivation during the folding of alkaline phosphatase. J Biol Chem 274:4532-6
Gershenson, A; Gafni, A; Steel, D (1998) Comparison of the time-resolved absorption and phosphorescence from the tryptophan triplet state in proteins in solution. Photochem Photobiol 67:391-8
Bergenhem, N C; Lee, S J; Gafni, A (1997) The stable, inactive but reactivatable, unfolding intermediate of rat muscle sarcoplasmic reticulum Ca(2+)-ATPase differs from the age-modified form of this protein. J Gerontol A Biol Sci Med Sci 52:B240-4
Gafni, A (1997) Structural modifications of proteins during aging. J Am Geriatr Soc 45:871-80
Subramaniam, V; Steel, D G; Gafni, A (1996) In vitro renaturation of bovine beta-lactoglobulin A leads to a biologically active but incompletely refolded state. Protein Sci 5:2089-94

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