Unraveling Photoexcited Conformational Changes of Bacteriorhodopsin by Time Resolved Electron Paramagnetic Resonance Spectroscopy

By means of time-resolved electron paramagnetic resonance (EPR) spectroscopy, the photoexcited structural changes of site-directed spin-labeled bacteriorhodopsin are studied. A complete set of cysteine mutants of the C-D loop, positions 100–107, and of the E-F loop, including the first α-helical tur...

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Veröffentlicht in:	Biophysical journal 2000-03, Vol.78 (3), p.1519-1530
Hauptverfasser:	Rink, Thomas, Pfeiffer, Matthias, Oesterhelt, Dieter, Gerwert, Klaus, Steinhoff, Heinz-Jürgen
Format:	Artikel
Sprache:	eng
Schlagworte:	Amino Acid Sequence Amino Acid Substitution Bacteria Bacteriorhodopsins - chemistry Bacteriorhodopsins - radiation effects Biochemistry Electron Spin Resonance Spectroscopy - methods Models, Molecular Mutagenesis, Site-Directed Photochemistry Protein Conformation - radiation effects Protein Structure, Secondary Proteins Recombinant Proteins - chemistry Recombinant Proteins - radiation effects Spectrum analysis Spin Labels Time Factors
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