Literature DB >> 10961509

Bacteriorhodopsin: the functional details of a molecular machine are being resolved

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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.

Year:  2000        PMID: 10961509     DOI: 10.1016/s0301-4622(99)00154-4

Source DB:  PubMed          Journal:  Biophys Chem        ISSN: 0301-4622            Impact factor:   2.352


  16 in total

1.  Vibrational spectroscopy of an algal Phot-LOV1 domain probes the molecular changes associated with blue-light reception.

Authors:  K Ataka; P Hegemann; J Heberle
Journal:  Biophys J       Date:  2003-01       Impact factor: 4.033

2.  Monitoring light-induced structural changes of Channelrhodopsin-2 by UV-visible and Fourier transform infrared spectroscopy.

Authors:  Eglof Ritter; Katja Stehfest; Andre Berndt; Peter Hegemann; Franz J Bartl
Journal:  J Biol Chem       Date:  2008-10-16       Impact factor: 5.157

3.  Hydration dynamics in a partially denatured ensemble of the globular protein human alpha-lactalbumin investigated with molecular dynamics simulations.

Authors:  Neelanjana Sengupta; Simon Jaud; Douglas J Tobias
Journal:  Biophys J       Date:  2008-09-05       Impact factor: 4.033

4.  The role of protein-solvent hydrogen bond dynamics in the structural relaxation of a protein in glycerol versus water.

Authors:  Mounir Tarek; Douglas J Tobias
Journal:  Eur Biophys J       Date:  2008-04-22       Impact factor: 1.733

5.  Water molecules and hydrogen-bonded networks in bacteriorhodopsin--molecular dynamics simulations of the ground state and the M-intermediate.

Authors:  Sergei Grudinin; Georg Büldt; Valentin Gordeliy; Artur Baumgaertner
Journal:  Biophys J       Date:  2005-02-24       Impact factor: 4.033

6.  Regio-selective detection of dynamic structure of transmembrane alpha-helices as revealed from (13)C NMR spectra of [3-13C]Ala-labeled bacteriorhodopsin in the presence of Mn2+ ion.

Authors:  S Tuzi; J Hasegawa; R Kawaminami; A Naito; H Saitô
Journal:  Biophys J       Date:  2001-07       Impact factor: 4.033

7.  Site-directed mutagenesis combined with oxidative methionine labeling for probing structural transitions of a membrane protein by mass spectrometry.

Authors:  Yan Pan; Leonid Brown; Lars Konermann
Journal:  J Am Soc Mass Spectrom       Date:  2010-08-13       Impact factor: 3.109

8.  Light-induced Difference Terahertz Spectroscopy.

Authors:  Y C Shen; P C Upadhya; A G Davies; E H Linfield
Journal:  J Biol Phys       Date:  2003-06       Impact factor: 1.365

9.  Dynamics of reassembled thioredoxin studied by magic angle spinning NMR: snapshots from different time scales.

Authors:  Jun Yang; Maria Luisa Tasayco; Tatyana Polenova
Journal:  J Am Chem Soc       Date:  2009-09-30       Impact factor: 15.419

10.  Proton transfer dynamics on the surface of the late M state of bacteriorhodopsin.

Authors:  Esther Nachliel; Menachem Gutman; Jörg Tittor; Dieter Oesterhelt
Journal:  Biophys J       Date:  2002-07       Impact factor: 4.033

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