Literature DB >> 10410806

Closing in on bacteriorhodopsin: progress in understanding the molecule.

U Haupts1, J Tittor, D Oesterhelt.   

Abstract

Bacteriorhodopsin is the best understood ion transport protein and has become a paradigm for membrane proteins in general and transporters in particular. Models up to 2.5 A resolution of bacteriorhodopsin's structure have been published during the last three years and are basic for understanding its function. Thus one focus of this review is to summarize and to compare these models in detail. Another focus is to follow the protein through its catalytic cycle in summarizing more recent developments. We focus on literature published since 1995; a comprehensive series of reviews was published in 1995 (112).

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Year:  1999        PMID: 10410806     DOI: 10.1146/annurev.biophys.28.1.367

Source DB:  PubMed          Journal:  Annu Rev Biophys Biomol Struct        ISSN: 1056-8700


  106 in total

1.  Unraveling photoexcited conformational changes of bacteriorhodopsin by time resolved electron paramagnetic resonance spectroscopy.

Authors:  T Rink; M Pfeiffer; D Oesterhelt; K Gerwert; H J Steinhoff
Journal:  Biophys J       Date:  2000-03       Impact factor: 4.033

2.  Structure of the bacteriorhodopsin mutant F219L N intermediate revealed by electron crystallography.

Authors:  J Vonck
Journal:  EMBO J       Date:  2000-05-15       Impact factor: 11.598

3.  Control of the pump cycle in bacteriorhodopsin: mechanisms elucidated by solid-state NMR of the D85N mutant.

Authors:  Mary E Hatcher; Jingui G Hu; Marina Belenky; Peter Verdegem; Johan Lugtenburg; Robert G Griffin; Judith Herzfeld
Journal:  Biophys J       Date:  2002-02       Impact factor: 4.033

4.  Energy transfer from tryptophane amino acid residues to retinal in a bacteriorhodopsin molecule within a femtosecond timescale.

Authors:  O A Dzhemesyuk; S A Antipin; F E Gostev; I B Fedorovich; O M Sarkisov; M A Ostrovskii
Journal:  Dokl Biochem Biophys       Date:  2002 Jan-Feb       Impact factor: 0.788

5.  Time-resolved detection of transient movement of helices F and G in doubly spin-labeled bacteriorhodopsin.

Authors:  N Radzwill; K Gerwert; H J Steinhoff
Journal:  Biophys J       Date:  2001-06       Impact factor: 4.033

6.  Unfolding pathways of native bacteriorhodopsin depend on temperature.

Authors:  Harald Janovjak; Max Kessler; Dieter Oesterhelt; Hermann Gaub; Daniel J Müller
Journal:  EMBO J       Date:  2003-10-01       Impact factor: 11.598

7.  The structures of the active center in dark-adapted bacteriorhodopsin by solution-state NMR spectroscopy.

Authors:  Heiko Patzelt; Bernd Simon; Antonius terLaak; Brigitte Kessler; Ronald Kühne; Peter Schmieder; Dieter Oesterhelt; Hartmut Oschkinat
Journal:  Proc Natl Acad Sci U S A       Date:  2002-07-15       Impact factor: 11.205

8.  Tyr-199 and charged residues of pharaonis Phoborhodopsin are important for the interaction with its transducer.

Authors:  Yuki Sudo; Masayuki Iwamoto; Kazumi Shimono; Naoki Kamo
Journal:  Biophys J       Date:  2002-07       Impact factor: 4.033

9.  Stability of bacteriorhodopsin alpha-helices and loops analyzed by single-molecule force spectroscopy.

Authors:  Daniel J Müller; Max Kessler; Filipp Oesterhelt; Clemens Möller; Dieter Oesterhelt; Hermann Gaub
Journal:  Biophys J       Date:  2002-12       Impact factor: 4.033

Review 10.  Structure, dynamics and reactions of protein hydration water.

Authors:  Jeremy C Smith; Franci Merzel; Ana-Nicoleta Bondar; Alexander Tournier; Stefan Fischer
Journal:  Philos Trans R Soc Lond B Biol Sci       Date:  2004-08-29       Impact factor: 6.237

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