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Forisomes: Mechano-proteins that exert force in contraction and expansion

 
: Knoblauch, M.; Noll, G.A.; Prüfer, D.; Jaag, H.; Fontanellaz, M.E.; Schneider-Hüther, I.; Bel, A.J. van; Peters, W.S.

Laudon, M. ; Nano Science and Technology Institute -NSTI-:
NSTI Nanotechnology Conference and Trade Show 2004. Vol.1 : NSTI Nanotech 2004 ; March 7 - 11, 2004, Boston Sheraton Hotel, Boston, Massachusetts, USA ; includes 7th International Conference on Modeling and Simulation of Microsystems, MSM 2004, 4th International Conference on Computational Nanoscience and Technology, ICCN 2004, 2004 Workshop on Compact Modeling, WCM 2004 ; technical proceedings
Boston: NSTI, 2004
ISBN: 0-9728422-9-2
ISBN: 0-9728422-5-X
ISBN: 0-9728422-6-8
pp.1-2
Nanotechnology Conference and Trade Show (Nanotech) <2004, Boston/Mass.>
International Conference on Modeling and Simulation of Microsystems (MSM) <7, 2004, Boston/Mass.>
International Conference on Computational Nanoscience and Technology (ICCN) <4, 2004, Boston/Mass.>
Workshop on Compact Modeling (WCM) <2004, Boston/Mass.>
English
Conference Paper
Fraunhofer IME ()

Abstract
Motor-proteins are the basis of the dynamic three dimensional organization of the living cell. Most motor-proteins are driven by energetically favorable reactions such as ATP hydrolysis. We here describe anisotropic contractility in forisomes, protein bodies from higher plant cells, that is energized by changes of the free Ca2+ concentration in the nanomolar range and, alternatively, by alterations in pH. The rapid reaction is reversible; mechanic forces of similar magnitude are exerted in contraction and expansion. Individual forisomes can be isolated and kept fully functional in vitro. Forisomes represent a previously unknown class of mechano-protein with properties that invite their use in micro- and nanobiotechnological devices.

: http://publica.fraunhofer.de/documents/N-37914.html