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Journal article

Molecularly resolved protein electromechanical properties.

Abstract:
Previous work has shown that protein molecules can be trapped between the conductive surfaces presented by a metal-coated AFM probe and an underlying planar substrate where their molecule-specific conductance characteristics can be assayed. Herein, we demonstrate that transport across such a derived metal-protein-electrode junction falls within three, pressure-dependent, regimes and, further, that pressure-dependent conductance can be utilized in analyzing temporal variations of protein fold. Specifically, the electronic and mechanical properties of the metalloprotein azurin have been characterized under conditions of anisotropic vertical compression through the use of a conducting atomic force microscope (CP-AFM). By utilizing the ability of azurin to chemically self-assemble on the gold surface presented either by the apex of a suitably coated AFM probe or a planar metallic surface, molecular-level transport characteristics are assayable. Under conditions of low force, typically less than 2 nN, the weak physical and electronic coupling between the protein and the conducting contacts impedes tunneling and leads to charge buildup followed by dielectric breakdown. At slightly increased force, 3-5 nN, the copper protein exhibits temporal electron occupation with observable negative differential resistance, while the redox-inactive zinc mutant does not. At imposed loads greater than 5 nN, appreciable electron tunneling can be detected even at low bias for both the redox-active and -inactive species. Dynamic current-voltage characteristics have been recorded and are well-described by a modified Simmons tunneling model. Subsequent analyses enable the electron tunneling barrier height and barrier length to be determined under conditions of quantified vertical stress. The variance observed describes, in essence, the protein's mechanical properties within the confines of the tunnel junction.
Publication status:
Published

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Publisher copy:
10.1021/jp070262o

Authors


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Institution:
University of Oxford
Division:
MPLS
Department:
Chemistry
Sub department:
Inorganic Chemistry
Role:
Author


Journal:
journal of physical chemistry. B More from this journal
Volume:
111
Issue:
30
Pages:
9062-9068
Publication date:
2007-08-01
DOI:
EISSN:
1520-5207
ISSN:
1520-6106


Language:
English
Keywords:
Pubs id:
pubs:33925
UUID:
uuid:44e5498d-0969-4149-96fb-5981d916d022
Local pid:
pubs:33925
Source identifiers:
33925
Deposit date:
2012-12-19

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