Title of article
Bacteriorhodopsin: the functional details of a molecular machine are being resolved
Author/Authors
Joachim Heberle، نويسنده , , J?rg Fitter، نويسنده , , Hans Jürgen Sass، نويسنده , , Georg Büldt، نويسنده ,
Issue Information
روزنامه با شماره پیاپی سال 2000
Pages
20
From page
229
To page
248
Abstract
The photon-driven proton translocator bacteriorhodopsin is considered to be the best understood membrane protein so far. It is nowadays regarded as a model system for photosynthesis, ion pumps and seven transmembrane receptors. The profound knowledge came from the applicability of a variety of modern biophysical techniques which have often been further developed with research on bacteriorhodopsin and have delivered major contributions also to other areas. Most prominent examples are electron crystallography, solid-state NMR spectroscopy and time-resolved vibrational spectroscopy. The recently introduced method of crystallising a membrane protein in the lipidic cubic phase led to high-resolution structures of ground state bacteriorhodopsin and some of the photocycle intermediates. This achievement in combination with spectroscopic results will strongly advance our understanding of the functional mechanism of bacteriorhodopsin on the atomic level. We present here the current knowledge on specific aspects of the structural and functional dynamics of the photoreaction of bacteriorhodopsin with a focus on techniques established in our institute.
Keywords
Retinal protein , X-ray crystallography , Proton transfer , Neutron scattering , FT-IR spectroscopy
Journal title
Biophysical Chemistry
Serial Year
2000
Journal title
Biophysical Chemistry
Record number
1112835
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