Folding and Dynamics of A Bi-Domain Enzyme

Mas, Maria T.

Abstract

Funding Agency

• Agency: National Institute of Health (NIH)
• Institute: National Institute of General Medical Sciences (NIGMS)
• Type: Research Project (R01)
• Project #: 1R01GM041360-01
• Application #: 3299517
• Study Section: Biophysics and Biophysical Chemistry A Study Section (BBCA)
• Project Start: 1988-12-01
• Project End: 1991-11-30
• Budget Start: 1988-12-01
• Budget End: 1989-11-30
• Support Year: 1
• Fiscal Year: 1989

Institution

• Name: City of Hope/Beckman Research Institute
• City: Duarte
• State: CA
• Country: United States
• Zip Code: 91010

Publications

Szpikowska, B K; Mas, M T (1996) Urea-induced equilibrium unfolding of single tryptophan mutants of yeast phosphoglycerate kinase: evidence for a stable intermediate. Arch Biochem Biophys 335:173-82

Beechem, J M; Sherman, M A; Mas, M T (1995) Sequential domain unfolding in phosphoglycerate kinase: fluorescence intensity and anisotropy stopped-flow kinetics of several tryptophan mutants. Biochemistry 34:13943-8

Sherman, M A; Beechem, J M; Mas, M T (1995) Probing intradomain and interdomain conformational changes during equilibrium unfolding of phosphoglycerate kinase: fluorescence and circular dichroism study of tryptophan mutants. Biochemistry 34:13934-42

Szpikowska, B K; Beechem, J M; Sherman, M A et al. (1994) Equilibrium unfolding of yeast phosphoglycerate kinase and its mutants lacking one or both native tryptophans: a circular dichroism and steady-state and time-resolved fluorescence study. Biochemistry 33:2217-25

Haran, G; Haas, E; Szpikowska, B K et al. (1992) Domain motions in phosphoglycerate kinase: determination of interdomain distance distributions by site-specific labeling and time-resolved fluorescence energy transfer. Proc Natl Acad Sci U S A 89:11764-8

Beechem, J M; Haas, E (1989) Simultaneous determination of intramolecular distance distributions and conformational dynamics by global analysis of energy transfer measurements. Biophys J 55:1225-36