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Scientific article
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High-field EPR and site-directed spin labeling reveal a periodical polarity profile: The sequence 88 to 94 of the phototransducer NpHtrII in complex with sensory rhodopsin, NpSRII

Published inApplied magnetic resonance, vol. 30, p. 359-372
Publication date2006-06
Abstract

Taking advantage of the improved spectral resolution of high-field electron paramagnetic resonance (EPR) at 95 GHz/3.4 T as compared to conventional X-band EPR (9.5 GHz/0.34 T), detailed information on the polarity profile in a protein-protein interface is obtained. Nitroxide spin label side chains are introduced at positions 88 to 94 in the AS-1 sequence of the membrane adjacent HAMP domain of the transducer protein, NpHtrII, which is reconstituted in complex with sensory rhodopsin, NpSRII fromNatronobacterium pharaonis. Position-dependent variations of the values of the nitroxide magnetic tensor componentsgxx andAzz suggest that the spin label side chains at positions 88 to 93 of AS-1 are located between a hydrophobic and a hydrophilic microenvironment. The observed periodicity of the polarity properties of the respective spin label microenvironment agrees with an α-helical secondary structure of this part of AS-1 and validates a recently published molecular model which locates residues 88 and 91 in the interface between helices F and G of NpSRII and AS-1 of NpHtrII close to the cytoplasmic lipid-water interface.

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Affiliation Not a UNIGE publication
Citation (ISO format)
BRUTLACH, H. et al. High-field EPR and site-directed spin labeling reveal a periodical polarity profile: The sequence 88 to 94 of the phototransducer NpHtrII in complex with sensory rhodopsin, NpSRII. In: Applied magnetic resonance, 2006, vol. 30, p. 359–372.
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  • PID : unige:173890
ISSN of the journal0937-9347
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