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Observing the Mushroom-to-Brush Transition for Kinesin Proteins

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† Department of Biomedical Engineering, Columbia University, 1210 Amsterdam Avenue, New York, New York 10027, United States
‡ Columbia Business School, 3022 Broadway, New York, New York 10027, United States
*E-mail: [email protected]. Phone: +1 212 854 7749.
Cite this: Langmuir 2013, 29, 49, 15142–15145
Publication Date (Web):November 22, 2013
https://doi.org/10.1021/la4030712
Copyright © 2013 American Chemical Society
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    Abstract

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    The height of polymers grafted to a surface is predicted to be constant at low densities (“mushroom” regime) and increase with the third root of the polymer surface density at high densities (“brush” regime). This mushroom-to-brush transition is explored with kinesin-1 proteins adhered to a surface at controlled densities. The kinesin height is measured by attaching fluorescently labeled microtubules to the kinesins and determining their elevation using fluorescence interference contrast microscopy. Our measurements are consistent with a mushroom regime and a brush regime and a transition near the theoretically predicted density. The mushroom-to-brush transition may play a role in protein behavior in crowded cellular environments and may be exploited as a signal in intracellular regulation and mechanotransduction.

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    Detailed experimental methods, kinesin density measurements, and clustering Bayesian algorithm. This material is available free of charge via the Internet at http://pubs.acs.org.

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