Combining high-field EPR with site-directed spin labeling reveals unique information on proteins in action

Magnetic Resonance in Chemistry

Volumn 43, Issue SPEC. ISS., 2005, Pages

  Mobius K ^a   Savitsky, A ^a   Wegener, C ^b   Plato, M ^a   Fuchs, M ^a   Schnegg, A ^a   Dubinskii, A A ^c   Grishin, Y A ^d   Grigor'ev, I A ^e   Kuhn M ^b   Duche D ^f   Zimmermann, H ^g   Steinhoff, H J ^b  

^a FREIE UNIVERSITÄT BERLIN   (Germany)

^b UNIVERSITY OF OSNABRÜCK   (Germany)

^c SEMENOV INSTITUTE OF CHEMICAL PHYSICS   (Russian Federation)

^d INSTITUTE OF CHEMICAL KINETICS AND COMBUSTION   (Russian Federation)

^e N N VOROZHTSOV NOVOSIBIRSK INSTITUTE OF ORGANIC CHEMISTRY   (Russian Federation)

^f CNRS   (France)

^g MAX PLANCK INSTITUTE FOR MEDICAL RESEARCH   (Germany)

Author keywords

High field EPR; Ion channel formation; Proton transport; Site directed spin labeling; Transmembrane proteins

Indexed keywords

ELECTRON SPIN RESONANCE SPECTROSCOPY; ESCHERICHIA COLI; HYDROGEN BONDS; IONS; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; PARAMAGNETISM; PHOTOSYNTHESIS; PROTEINS; X RAY CRYSTALLOGRAPHY;

CHANNEL FORMATION; HIGH-FIELD; HIGH-FIELD ELECTRON PARAMAGNETIC RESONANCE; ION CHANNEL; ION-CHANNEL FORMATION; PROTON TRANSPORT; SITE-DIRECTED SPIN LABELING; TRANS-MEMBRANE PROTEINS; TRANSFER PROCESS; TRANSMEMBRANE PROTEINS;

PARAMAGNETIC RESONANCE;

EID: 27644581213     PISSN: 07491581     EISSN: None     Source Type: Journal    
DOI: 10.1002/mrc.1690     Document Type: Article

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