ArticleBiophysical journal1999
Location of a cation-binding site in the loop between helices F and G of bacteriorhodopsin as studied by 13C NMR.
Article in Biophysical journal, 1999. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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12 citing papers in PubMed.
- Combination of extended X-ray absorption fine structure spectroscopy with lipidic cubic phases for the study of cation binding in bacteriorhodopsin.European biophysics journal : EBJ · 2011Article
- Chemical shift tensor - the heart of NMR: Insights into biological aspects of proteins.Progress in nuclear magnetic resonance spectroscopy · 2010Review
- A quantitative XANES analysis of the calcium high-affinity binding site of the purple membrane.Biophysical journal · 2004Article
- Glutamic acid residues of bacteriorhodopsin at the extracellular surface as determinants for conformation and dynamics as revealed by site-directed solid-state 13C NMR.Biophysical journal · 2004Article
- Proton transfer reactions in native and deionized bacteriorhodopsin upon delipidation and monomerization.Biophysical journal · 2003Article
- Specific binding sites for cations in bacteriorhodopsin.Biophysical journal · 2001Article
- 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.Biophysical journal · 2001Article
- Time-resolved Fourier transform infrared spectroscopy of the polarizable proton continua and the proton pump mechanism of bacteriorhodopsin.Biophysical journal · 2001Article
- Conformational transitions and fibrillation mechanism of human calcitonin as studied by high-resolution solid-state 13C NMR.Protein science : a publication of the Protein Society · 2000Article
- Conformational changes of bacteriorhodopsin along the proton-conduction chain as studied with (13)C NMR of [3-(13)C]Ala-labeled protein: arg(82) may function as an information mediator.Biophysical journal · 1999Article
- Long-distance effects of site-directed mutations on backbone conformation in bacteriorhodopsin from solid state NMR of [1-13C]Val-labeled proteins.Biophysical journal · 1999Article
- Binding of calcium ions to bacteriorhodopsin.Biophysical journal · 1999Article
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9 authors.
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Abstract
The high-affinity cation-binding sites of bacteriorhodopsin (bR) were examined by solid-state 13C NMR of samples labeled with [3-13C]Ala and [1-13C]Val. We found that the 13C NMR spectra of two kinds of blue membranes, deionized (pH 4) and acid blue at pH 1.2, were very similar and different from that of the native purple membrane. This suggested that when the surface pH is lowered, either by removal of cations or by lowering the bulk pH, substantial change is induced in the secondary structure of the protein. Partial replacement of the bound cations with Na+, Ca2+, or Mn2+ produced additional spectral changes in the 13C NMR spectra. The following conclusions were made. First, there are high-affinity cation-binding sites in both the extracellular and the cytoplasmic regions, presumably near the surface, and one of the preferred cation-binding sites is located at the loop between the helix F and G (F-G loop) near Ala196, consistent with the 3D structure of bR from x-ray diffraction and cryoelectron microscopy. Second, the bound cations undergo rather rapid exchange (with a lifetime shorter than 3 ms) among various types of cation-binding sites. As expected from the location of one of the binding sites, cation binding induced conformational alteration of the F-G interhelical loop.
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