期刊
PHOTOCHEMISTRY AND PHOTOBIOLOGY
卷 83, 期 2, 页码 263-272出版社
WILEY
DOI: 10.1562/2006-07-05-RA-960
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The nature and kinetics of the conformational changes leading to the activated state of NpSRII/NpHtrII(157) were investigated by time-resolved electron paramagnetic resonance (TR-EPR) spectroscopy in combination with site-directed spin labeling (SDSL) on a series of spin labeled mutants of NpSRII. A structural rearrangement of the cytoplasmic moiety of NpSRII upon light activation was detected (helices B, C, F and G). The increase in distance between helices C and F in the M-trapped state of the complex observed in one double mutant is in line with the notion that an outward movement of helix F occurs upon receptor activation. The data obtained from the NpSRII/NpHtrII(157) complex reconstituted in purple membrane lipids are compared with those obtained from the X-ray structure of the late M-state of the complex which shows some discrepancies. The results are discussed in the context also of other biophysical and EPR experimental evidences.
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