QM/MM Study of Rhodopsin

Ute F. Röhrig, Christel Nonnenberg, Irmgard Frank (), Leonardo Guidoni and Ursula Röthlisberger
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Ute F. Röhrig: ETH Zürich, Laboratory of Inorganic Chemistry
Christel Nonnenberg: Department Chemie
Irmgard Frank: Department Chemie
Leonardo Guidoni: ETH Zürich, Laboratory of Inorganic Chemistry
Ursula Röthlisberger: ETH Zürich, Laboratory of Inorganic Chemistry

A chapter in High Performance Computing in Science and Engineering, Munich 2002, 2003, pp 127-134 from Springer

Abstract: Abstract The investigation of the first step of vision is a long-standing problem in theoretical chemistry [1]. It has been text-book knowledge for a long time [2,3,4], that irradiation of the retina protein rhodopsin with light in the visible range induces a cis-trans isomerization at the C11-C12 double bond of the chromophore, i.e. of the light-absorbing part of the protein (Fig. 1). However, it is extremely difficult to study the reaction mechanism in full detail on experimental basis. The consecutive signal transduction cascade that finally leads to a neuron signal also still poses many questions.

Keywords: Molecular Dynamic Simulation; Halo Bacterium; Classical Molecular Dynamic; High Resolution Crystal Structure; Protein Binding Pocket (search for similar items in EconPapers)
Date: 2003
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DOI: 10.1007/978-3-642-55526-8_11

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