Douglas Swank

Professor, Biological Sciences

Dr. Swank has been a member of the RPI faculty since 2005. He heads a dynamic, multidisciplinary laboratory of students, staff, and post-docs. His laboratory investigates how muscle is able to power an amazingly wide variety of locomotory tasks and modulate heart function. Research focuses in the lab include determining how variation between muscle fiber types (e.g. slow versus fast-contracting fibers) is generated, the mechanisms behind muscle mechanical properties such as stretch activation, and muscle diseases such as hypertrophic cardiomyopathy. 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. His research team primarily uses Drosophila for their studies, due to Drosophila's ease of genetic manipulation and mechanically testable muscles. However, we have recently started using mammalian muscle types to gain further insights.

Dr Swank's lab has primarily focused on the role of myosin, the molecular motor that powers muscle contraction, in modulating muscle mechanical properties. 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. Besides myosin, the laboratory also investigates the function of other muscle proteins such as muscle LIM protein (MLP), actin and troponin C.

The lab investigates mechanisms behind several muscle and heart diseases such as familial hypertrophic cardiomyopathy (HCM) and distal arthrogryposis. FHC is an inherited genetic disease that is the leading cause of sudden cardiac arrest among young adults. The lab creates transgenic Drosophila models of these diseases and perform experiments to determine how these disease states alter the mechanical function of muscle and tp provide insights into possible treatments.

For more information about Dr. Swank's research and team members, visit the Swank laboratory web site:



B.S. University of Rochester, 1990, Biology

Ph.D., University of Pennsylvania, 1995, Physiology

Postdoctoral Fellow, San Diego State University, 2000, Drosophila Genetics

Postdoctoral Fellow, University of Vermont, 2005, Muscle Mechanics

Research Focus
  • Heart Disease
  • Muscle Disease
  • Cardiac Physiology
  • Muscle Physiology
  • Motor Proteins
  • Locomotion
  • Drosophila Genetics
Select Works
  • Our most recent work is listed below. A full publication list is available at:
  • Kronert, W.A., K.M. BellG, M.C. Viswanathan, G.C. Melkani, A.S. Trujillo, A. Huang, A. Melkani, A. Cammarato, D.M. Swank, and S.I. Bernstein (2018) Prolonged cross-bridge binding triggers muscle dysfunction in a Drosophila model of myosin-based hypertrophic cardiomyopathy. elife. 7: e38064. (Comment in: Too much of a good thing. elife, 2018).
  • Glasheen, B.M., S. Ramanath, M. Patel, D. Sheppard, J.T. Puthawala, L.A. Riley, and D.M. Swank (2018) Five alternative myosin converter domains influence Drosophila muscle power, stretch activation, cross-bridge kinetics and flight. Biophysical Journal. 114:1142-1152.
  • Glasheen, B.M., C.C. Eldred, L.C. Sullivan, C. Zhao, M.K. Reedy, R.J. Edwards, D.M. Swank (2017) Stretch activation properties of Drosophila and Lethocerus indirect flight muscle suggest similar calcium dependent mechanisms. Am. J. Physiol. Cell Physiol. 313(6):C621-C631.
  • Suggs J.A., Melkani G.C., Glasheen B.M., Detor M.M., Melkani A., Marsan N.P., Swank D.M., Bernstein S.I. (2017) A Drosophila model of dominant inclusion body myopathy type 3 shows diminished myosin kinetics that reduce muscle power and yield myofibrillar defects. Disease Models & Mechanisms 10(6):761-771.
  • Zhao C., Swank D.M. (2017) The Drosophila indirect flight muscle myosin heavy chain isoform is insufficient to transform the jump muscle into a highly stretch-activated muscle type. American Journal of Physiology: Cell Physiology 312(2):C111-C118.
  • Achal M., Trujillo A.S., Melkani G.C., Farman G.P., Ocorr K., Viswanathan M.C., Kaushik G., Newhard C.S., Glasheen B.M., Melkani A., Suggs J.A., Moore J.R., Swank D.M., Bodmer R., Cammarato A., and Bernstein S.I. (2016) A Restrictive Cardiomyopathy Mutation in an Invariant Proline at the Myosin Head/Rod Junction Enhances Head Flexibility and Function, Yielding Muscle Defects in Drosophila. Journal of Molecular Biology 428(11):2446-61.
  • Koppes R.A., Swank D.M., Corr D.T. (2015) A new experimental model for force enhancement: steady-state and transient observations of the Drosophila jump muscle. American Journal of Physiology: Cell Physiology 309(8):C551-7.