Image of David Altman

Contact Information

Collins Science Center 313
900 State Street
Salem  Oregon  97301


PhD, Physics, Stanford University, 2006

BA, Physics, The University of Chicago, 2000


The inside of a cell is crowded and highly organized. It is because of its ordered state that a cell is a dynamic and exciting environment. Molecular motors are the biomolecules that generate force and motion, and thus do the work that is necessary to maintain the cell’s organization. Research in my lab seeks to understand how the molecular motor myosin functions in the cell by taking a two-fold approach. The first approach is to study myosins outside of the cell (in vitro). This allows us to reduce the complexity of the experimental system, but we must take the results from these experiments and extrapolate in order to understand how the motor actually functions inside the cell. The second approach we take is to study myosins inside the cell (in vivo). This means that the system is more complicated, with many other biomolecules complicating our experiment, but it also means that it is easier to understand the physiological relevance. We conduct studies at a variety of size scales, ranging from studies of individual purified motors (1 billionth of a meter) to single cells (1 millionth of a meter) to muscle fibers (1 thousandth of a meter).


Introductory Physics I and its associated lab PHYS 221 and 221Y

Research Experience in Physics PHYS 360

Research Seminar I PHYS 495

Physical Biology of the Cell PHYS 250

College Colloquium, Knitting Culture IDS 101

Advanced Techniques in Experimental Physics PHYS 396W 


Hewage, Navindi, and D. Altman, A role for myosin VI in retinal pigment epithelium phagocytosis, Biochemical and biophysical research communications, (2018) in press.

de Souza Leite, Felipe, Fabio C. Minozzo, David Altman, and Dilson E. Rassier. “Microfluidic perfusion shows intersarcomere dynamics within single skeletal muscle myofibrils.” Proceedings of the National Academy of Sciences (2017): 201700615.

Altman, David. “Cell Culture Protocols, HeLa and CHO Cells.” WHOAS: Woods Hole Open Access Server, MBLWHOI Library (2017) 

Minozzo, Fábio C., David Altman, and Dilson E. Rassier. "MgADP activation contributes to force enhancement during fast stretch of isolated skeletal myofibrils." Biochemical and biophysical research communications 463.4 (2015): 1129-1134. 

Altman, David, Fabio C. Minozzo, and Dilson E. Rassier. "Thixotropy and rheopexy of muscle fibers probed using sinusoidal oscillations." PloS one 10.4 (2015): e0121726.

Daniel, R., A.T. Koll, and D. Altman, Force dependence of phagosome trafficking in retinal pigment epithelial cells, Optical Trapping and Optical Micromanipulation XI, edited by Kishan Dholakia, Gabriel C. Spalding, Proc. of SPIE, 2014. 9164:916435.

Altman, D. Mechanism of myosin work and motility, in: Roberts GC. Encyclopedia of Biophysics. Heidelberg, Springer; 2012.

Altman, D. Fundamental properties and structure of myosin, in: Roberts GC. Encyclopedia of Biophysics. Heidelberg, Springer; 2012.

Altman, D., D. Goswami, T. Hasson, J.A. Spudich, and S. Mayor, Precise positioning of myosin VI on endocytic vesicles. PLoS Biology, 2007. 5(8): e210.

Bryant, Z., D. Altman, J.A. Spudich, The power stroke of myosin VI and the basis of reverse directionailty. Proc. Natl. Acad. Sci. USA, 2007. 104, 722-777.


Named a Fellow for Scialog: Molecules Come to Life by the Research Corporation for Science Advancement and the Gordon and Betty Moore Foundation, 2014

co-PI on Optics and Photonics Training for Inquisitive eXperimentalists (OPTIX), collaborative with Michaela Kleinert and Rick Watkins, Integrative Activities in Physics (IAP) program, National Science Foundation, 2015, funded.

The role of force in regulating the function of myosin motors, College Research Program for Life Sciences Grant, M.J. Murdock Charitable Trust, 2014.

Willamette University

Physics Department

Collins Science Center
Willamette University
900 State Street
Salem Oregon 97301 U.S.A.
503-370-6894 voice
503-370-6773 fax

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