Robust mechanobiological behavior emerges in heterogeneous myosin systems

Paul F. Egan, Jeffrey R. Moore, Allen J. Ehrlicher, David A. Weitz, Christian Schunn, Jonathan Cagan, Philip LeDuc
  • Proceedings of the National Academy of Sciences, September 2017, Proceedings of the National Academy of Sciences
  • DOI: 10.1073/pnas.1713219114

Improving biosystem performance by mixing myosin isoforms

What is it about?

We use a computational model to combine and simulate the force-velocity-energy properties of myosin motor proteins driving muscles and nanotechnologies. We show that certain combinations of two myosins working together have unique and advantageous properties in comparison to systems with only one type of myosin.

Why is it important?

The project is unique because we combine myosin types and use computational models to test myosins at a faster rate than biological experiments could accomplish. We then validate the high performing biosystems predicted computationally with laboratory experiments.

Perspectives

Professor Paul Egan (Author)
Texas Tech University System

The paper is particularly important because it combines engineering design methods, with computational biology, and bioengineering to investigate unique combinations of myosin motor proteins that are difficult to investigate using the tools of a single scientific discipline.

Read Publication

http://dx.doi.org/10.1073/pnas.1713219114

The following have contributed to this page: Professor Paul Egan