Douglas Swank

Douglas Swank

Dr. Swank has been a member of the RPI faculty since 2005. He heads a dynamic, multidisciplinary laboratory of students, staff, and post-docs. He teaches Human Physiology to undergraduate Biology majors and helps team teach various graduate courses. Dr. Swank’s laboratory investigates how muscle is able to power an amazingly wide variety of locomotory tasks and modulate heart function. The laboratory is also working to understand the mechanisms behind muscle disease states such as familial hypertrophic cardiomyopathy (FHC). FHC is an inherited genetic disease that is the leading cause of sudden cardiac arrest among young adults. One of his laboratory’s focus is to determine how variation between muscle fiber types (e.g. slow- versus fast-contracting fibers) is generated. An integrative approach is taken, starting with muscle genes and moving up in scale to protein expression and function, muscle mechanics, and whole organism studies. This comprehensive approach is possible by exploiting the unique genetic properties and transgenic techniques available for Drosophila. Drosophila is currently the only system that can be transgenically manipulated to express a specific myosin isoform or mutant myosin in a specific muscle type. The expressed myosin can be isolated from Drosophila to measure single and ensemble biochemical and biophysical molecular properties such as ATPase rate and actin sliding velocity. Laboratory members also measure mechanical properties (e.g. power, velocity and force) of isolated muscle fibers expressing transgenic myosin and relate altered fiber properties to changes in locomotion - such as flight ability. Some of the myosin structural regions Dr. Swank is investigating using Drosophila (e.g. the “converter” region) are hot spots for point mutations that lead to FHC. He is also directly studying the effects of point mutations that cause FHC on muscle performance by reproducing these mutations in transgenic Drosophila models. Besides myosin, the laboratory also investigates the function of other muscle proteins such as muscle LIM protein (MLP), actin and troponin C.

  • Ph.D. - University of Pennsylvania, 1995, Physiology; Postdoc - San Diego State University, Drosophila Genetics; Postdoc- University of Vermont, Muscle Mechanics

  • Eldred, C.C., A. Katzemich, M. Patel, B. Bullard and D.M. Swank (2014) The roles of troponin C isoforms in the mechanical function of Drosophila indirect flight muscle. Journal of Muscle Research and Cell Motility (in press)
  • Koppes R.A., D.M. Swank, and D.T. Corr (2014) A new experimental model to study force depression: the Drosophila jump muscle. Journal of Applied Physiology 116: 1543-1550.
  • Eldred, C.C., N. Naber, R. Cooke, E. Pate, and D. M. Swank (2013) Conformational changes at the nucleotide site in the presence of bound ADP do not set the velocity of fast Drosophila myosins. Journal of Muscle Research and Cell Motility: 34:35-42.
  • Zhao, C. and D.M. Swank (2013) An embryonic myosin isoform enables stretch activation and cyclical power in Drosophila jump muscle. Biophysical Journal 104:2662-2670.
  • Wang, Q., C.S. Newhard, S. Ramanath, D. Sheppard, and D.M. Swank (2013) An embryonic myosin converter domain influences Drosophila indirect flight muscle stretch activation, power generation and flight. Journal of Experimental Biology 217:290-298.
  • Swank, D.M. (2012) Mechanical analysis of Drosophila indirect flight and jump muscles. Methods 56:69-77.
  • Wang, Q., C. Zhao and D.M. Swank (2011) Calcium and stretch-activation modulate power generation in Drosophila flight muscle. Biophyical Journal 101: 2207-2213.
  • Ramanath, S., Q. Wang, W. A. Kronert, S. I. Bernstein and D. M. Swank (2011) Disrupting the myosin converter-relay interface impairs Drosophila indirect flight muscle performance. Biophysical Journal 101: 1114-1122.
  • Clark, K.A., H. Lesage, C. Zhao, M. Beckerle and D. M. Swank (2011) Deletion of Drosophila muscle LIM protein decreases flight muscle stiffness and power generation. Amer. J. Physiol.-Cell 301:C373-C382
  • Purcell, T. J., N. Naber, K. Franks-Skiba, A. R. Dunn, C. C. Eldred, C. L. Berger, A. Malnasi-Csizmadia, J. A. Spudich, D. M. Swank, E. Pate, and R. Cooke. (2011). Nucleotide pocket thermodynamics measured by EPR reveal how energy partitioning relates myosin speed to efficiency. J. Mol. Biol. 407:79-91.