Biophysical Studies of the Myosin Atpase

Shriver, John W.

Abstract

Funding Agency

• Agency: National Institute of Health (NIH)
• Institute: National Institute of Arthritis and Musculoskeletal and Skin Diseases (NIAMS)
• Type: Modified Research Career Development Award (K04)
• Project #: 5K04AR001788-05
• Application #: 3071358
• Study Section: Molecular and Cellular Biophysics Study Section (BBCA)
• Project Start: 1988-09-01
• Project End: 1993-08-31
• Budget Start: 1992-09-01
• Budget End: 1993-08-31
• Support Year: 5
• Fiscal Year: 1992

Institution

• Name: Southern Illinois University Carbondale
• Type: Schools of Arts and Sciences
• DUNS #: 939007555
• City: Carbondale
• State: IL
• Country: United States
• Zip Code: 62901

Publications

Edmondson, S; Khan, N; Shriver, J et al. (1991) The solution structure of motilin from NMR distance constraints, distance geometry, molecular dynamics, and an iterative full relaxation matrix refinement. Biochemistry 30:11271-9

Khan, N; Graslund, A; Ehrenberg, A et al. (1990) Sequence-specific 1H NMR assignments and secondary structure of porcine motilin. Biochemistry 29:5743-51

Shriver, J W; Kamath, U (1990) Differential scanning calorimetry of the unfolding of myosin subfragment 1, subfragment 2, and heavy meromyosin. Biochemistry 29:2556-64

Shriver, J W (1990) Differential scanning calorimetry of a conformational transition in heavy meromyosin. Arch Biochem Biophys 283:472-5