Calorimetric Study of Protein Conformational Dynamics

Tsong, Tian Y.

Abstract

Funding Agency

• Agency: National Institute of Health (NIH)
• Institute: National Institute of General Medical Sciences (NIGMS)
• Type: Research Project (R01)
• Project #: 5R01GM037304-02
• Application #: 3292623
• Study Section: Biophysics and Biophysical Chemistry A Study Section (BBCA)
• Project Start: 1986-01-01
• Project End: 1990-12-31
• Budget Start: 1987-01-01
• Budget End: 1987-12-31
• Support Year: 2
• Fiscal Year: 1987

Institution

• Name: Johns Hopkins University
• Type: Schools of Medicine
• DUNS #: 045911138
• City: Baltimore
• State: MD
• Country: United States
• Zip Code: 21218

Publications

Chen, H M; Markin, V S; Tsong, T Y (1992) pH-induced folding/unfolding of staphylococcal nuclease: determination of kinetic parameters by the sequential-jump method. Biochemistry 31:1483-91

Chen, H M; Markin, V S; Tsong, T Y (1992) Kinetic evidence of microscopic states in protein folding. Biochemistry 31:12369-75

Chen, H M; You, J L; Markin, V S et al. (1991) Kinetic analysis of the acid and the alkaline unfolded states of staphylococcal nuclease. J Mol Biol 220:771-8

Bertazzon, A; Tian, G H; Lamblin, A et al. (1990) Enthalpic and entropic contributions to actin stability: calorimetry, circular dichroism, and fluorescence study and effects of calcium. Biochemistry 29:291-8

Bertazzon, A; Tsong, T Y (1990) Effects of ions and pH on the thermal stability of thin and thick filaments of skeletal muscle: high-sensitivity differential scanning calorimetric study. Biochemistry 29:6447-52

Bertazzon, A; Tsong, T Y (1990) Study of effects of pH on the stability of domains in myosin rod by high-resolution differential scanning calorimetry. Biochemistry 29:6453-9

Bertazzon, A; Tsong, T Y (1989) High-resolution differential scanning calorimetric study of myosin, functional domains, and supramolecular structures. Biochemistry 28:9784-90