Published November 2009 | Version v1
Journal article

Detecting conformational change by current transport in proteins: The case of bacteriorhodopsin monolayers

  • 1. CNISM - via della Vasca Navale, 84, I-00146, Roma (Italy)
  • 2. Dipartimento di Ingegneria dell'innovazione. Universita del Salento, via Monteroni, I-73100 Lecce (Italy)

Description

Recent experiments on the light receptor bacteriorhodopsin have revealed the protein conductive properties and connected them to its sensing action. In particular it was shown that the super-Ohmic I-V characteristic acquired in dark, changes in the presence of green light, with an enhancement of current at increasing bias values. Here we propose a current transport model for proteins able to reproduce experimental data, mainly the dependence of current on their three dimensional (tertiary) structure. The model is based on a resistance network model and implements a tunneling mechanism of charge transfer between the amino-acids constituting the protein.

Availability note (English)

Available from http://dx.doi.org/10.1088/1742-6596/193/1/012107

Additional details

Publishing Information

Journal Title
Journal of Physics. Conference Series (Online)
Journal Volume
193
Journal Issue
1
Journal Page Range
[4 p.]
ISSN
1742-6596

Conference

Title
16. international conference on electron dynamics in semiconductors, optoelectronics and nanostructures
Acronym
EDISON 16
Dates
24-28 Aug 2009
Place
Montpellier (France)

INIS

Country of Publication
United Kingdom
Country of Input or Organization
International Atomic Energy Agency (IAEA)
INIS RN
42029960
Subject category
S75: CONDENSED MATTER PHYSICS, SUPERCONDUCTIVITY AND SUPERFLUIDITY;
Resource subtype / Literary indicator
Conference
Descriptors DEI
AMINO ACIDS; CHARGE TRANSPORT; CONFORMATIONAL CHANGES; ELECTRIC CONDUCTIVITY; ELECTRIC CURRENTS; RECEPTORS; TRANSPORT THEORY; TUNNEL EFFECT; VISIBLE RADIATION
Descriptors DEC
CARBOXYLIC ACIDS; CURRENTS; ELECTRICAL PROPERTIES; ELECTROMAGNETIC RADIATION; MEMBRANE PROTEINS; ORGANIC ACIDS; ORGANIC COMPOUNDS; PHYSICAL PROPERTIES; PROTEINS; RADIATIONS