Altman:Research: Difference between revisions

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| [[Image:opticaltrap.jpg|thumb|upright|170 px|Cartoon of a myosin attached to a bead that is held in an optical trap.]]
| [[Image:opticaltrap.jpg|thumb|center|170 px|Cartoon of a myosin attached to a bead that is held in an optical trap.]]
| [[Image:myosin1subclasses.jpg|thumb|upright|120 px|Image taken from [http://www.ncbi.nlm.nih.gov/pubmed/15037306 De La Cruz, et al.] ]]
| [[Image:myosin1subclasses.jpg|thumb|center|120 px|Image taken from [http://www.ncbi.nlm.nih.gov/pubmed/15037306 De La Cruz, et al.] ]]
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Revision as of 07:14, 24 November 2012


Department of Physics, Willamette University

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Single molecule studies of Acanthamoeba myosin 1

We are examining the force-sensitivity of Acanthamoeba myosin 1c (AM1C) activity. Class 1 myosins have been split into two subclasses. While subclass 2 myosins are hypothesized to have a force-dependent activity, subclass 1 myosins are not. Two subclass 2 myosins (Rat Myo1b and Mouse Myo1c) have been shown to have a high degree of force-sensitivity, but no subclass 1 myosin has yet been tested. To test the force sensitivity of AM1C, which is from subclass 1, we are using an optical trap, which allows us to apply picoNewton forces to single myosin motors.

Cartoon of a myosin attached to a bead that is held in an optical trap.
Image taken from De La Cruz, et al.


Retinal pigment epithelium phagocytosis