Paper
21 May 2001 Alternative designs for biosensors based on protein molecular motors
Author Affiliations +
Abstract
The differences in hydrophobicity produced by the e-beam patterning exposure of the surface of poly[(tert-butyl methacrylate)-co-(methyl methacrylate)] -a common e-beam and deep-UV resist, resulted in the selective attachment of heavy meromyosin on hydrophobic, unexposed surfaces. The movement of the actin filaments on myosin-rich and myosin- poor surfaces was statistically characterized in terms of velocity, acceleration, and angle of movement. The actin filaments have a smooth motion on myosin-rich surfaces and an uneven motion on myosin-poor surfaces. Interestingly, an excess of myosin sites has a slowing, albeit mild, effect on the motion of the action filaments. It was also found that the myosin-rich/myosin-poor boundary has an alignment- enforcement effect, especially for the filaments approaching the border from the myosin-rich side. Based on these results we discuss the feasibility of building purposefully designed molecular motor arrays and the testing of the hypothesis regarding the functioning of the biomolecular dynamic biodevice.
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Dan V. Nicolau, Sverre Myhra, and Florin Fulga "Alternative designs for biosensors based on protein molecular motors", Proc. SPIE 4265, Biomedical Instrumentation Based on Micro- and Nanotechnology, (21 May 2001); https://doi.org/10.1117/12.427974
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KEYWORDS
Proteins

Biosensors

Polymers

Control systems

Magnetism

Chemical elements

Lithium

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