corner
corner
APS » Journals » Phys. Rev. Lett. » Volume 95 » Issue 7
< Previous Article | Next Article >

Phys. Rev. Lett. 95, 078102 (2005) [4 pages]

Allosteric Control through Mechanical Tension

Download: PDF (923 kB) Buy this article Export: BibTeX or EndNote (RIS)

Brian Choi and Giovanni Zocchi
Department of Physics and Astronomy, University of California Los Angeles, Los Angeles, California 90095-1547, USA

Yim Wu1, Sum Chan1, and L. Jeanne Perry1,2
1UCLA-DOE Institute for Proteomics & Genomics, University of California Los Angeles, Los Angeles, California 90095-1547, USA
2Department of Molecular, Cell and Developmental Biology, University of California Los Angeles, Los Angeles, California 90095-1547, USA

Received 6 April 2005; published 8 August 2005

See accompanying Physics Focus

Conformational changes of proteins modulate their function. In allosteric control, the conformational change is induced by the binding of a signaling molecule. Here we insert a “molecular spring” on the enzyme guanylate kinase, to control the conformation of this protein. The stiffness of the spring can be varied externally, which allows one to exert a controlled mechanical tension between the two points on the protein’s surface where the spring is attached. We show that by applying and releasing the tension we can reversibly turn the enzyme off and on.

© 2005 The American Physical Society

URL:
http://link.aps.org/doi/10.1103/PhysRevLett.95.078102
DOI:
10.1103/PhysRevLett.95.078102
PACS:
87.15.He, 81.07.−b, 82.39.−k
 
< Previous Article | Next Article >