Artificial Allosteric Control of Maltose Binding Protein

Brian Choi, Giovanni Zocchi, Stephen Canale, Yim Wu, Sum Chan, and L. Jeanne Perry

Phys. Rev. Lett. 94, 038103 – Published 26 January 2005

Abstract

We demonstrate the allosteric control of a protein based on mechanical tension. When substrate binding is accompanied by a significant change of conformation of the protein, a mechanical tension favoring one or the other conformation will alter the binding affinity for the substrate. We have constructed a chimera where the two lobes of the maltose-binding protein are covalently coupled to the ends of a DNA oligomer. The mechanical tension on the protein is controlled externally by exploiting the difference in stiffness between single stranded and double stranded DNA. We report that the binding affinity of the protein for its substrates is significantly altered by the tension.

Received 2 April 2004

DOI:https://doi.org/10.1103/PhysRevLett.94.038103

Authors & Affiliations

Brian Choi and Giovanni Zocchi

Department of Physics and Astronomy, University of California–Los Angeles, Los Angeles, California 90095-1547, USA

Stephen Canale¹, Yim Wu², Sum Chan², and L. Jeanne Perry^1,2

¹Department of Molecular, Cell and Developmental Biology, University of California–Los Angeles, Los Angeles, California 90095-1547, USA
²UCLA-DOE Institute for Proteomics & Genomics, University of California–Los Angeles, Los Angeles, California 90095-1547, USA

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Issue

Vol. 94, Iss. 3 — 28 January 2005

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