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In vitro assays of molecular motors - impact of motor-surface interactions
University of Kalmar, School of Pure and Applied Natural Sciences.ORCID iD: 0000-0002-5889-7792
University of Kalmar, School of Pure and Applied Natural Sciences.
University of Kalmar, School of Pure and Applied Natural Sciences.
University of Kalmar, School of Pure and Applied Natural Sciences.
2008 (English)In: Frontiers in Bioscience, ISSN 1093-9946, Vol. 13, no May 1, 5732-5754 p.Article, review/survey (Other academic) Published
Abstract [en]

In many types of biophysical studies of both single molecules and ensembles of molecular motors the motors are adsorbed to artificial surfaces. Some of the most important assay systems of this type (in vitro motility assays and related single molecule techniques) will be briefly described together with an account of breakthroughs in the understanding of actomyosin function that have resulted from their use. A poorly characterized, but potentially important, entity in these studies is the mechanism of motor adsorption to surfaces and the effects of motor surface interactions on experimental results. A better understanding of these phenomena is also important for the development of commercially viable nanotechnological applications powered by molecular motors. Here, we will consider several aspects of motor surface interactions with a particular focus on heavy meromyosin (HMM) from skeletal muscle. These aspects will be related to heavy meromyosin structure and relevant parts of the vast literature on protein-surface interactions for non-motor proteins. An overview of methods for studying motor-surface interactions will also be given. The information is used as a basis for further development of a model for HMM-surface interactions and is discussed in relation to experiments where nanopatterning has been employed for in vitro reconstruction of actomyosin order. The challenges and potentials of this approach in biophysical studies, compared to the use of self-assembly of biological components into supramolecular protein aggregates (e. g. myosin filaments) will be considered. Finally, this review will consider the implications for further developments of motor-powered lab-on-a-chip devices.

Place, publisher, year, edition, pages
2008. Vol. 13, no May 1, 5732-5754 p.
National Category
Organic Chemistry
Research subject
Natural Science, Biomedical Sciences; Natural Science, Organic Chemistry
Identifiers
URN: urn:nbn:se:lnu:diva-5095OAI: oai:DiVA.org:lnu-5095DiVA: diva2:315076
Available from: 2010-04-28 Created: 2010-04-28 Last updated: 2015-09-14Bibliographically approved

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Månsson, AlfBalaz, MartinaTorres, Nuria AlbetRosengren, Johan
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CiteExportLink to record
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Citation style
  • apa
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  • modern-language-association-8th-edition
  • vancouver
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  • de-DE
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  • en-US
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  • nn-NO
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  • Other locale
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