tailieunhanh - Báo cáo Y học: Effect of adenosine 5¢-[b,c-imido]triphosphate on myosin head domain movements Saturation transfer EPR measurements without low-power phase setting

Conventional and saturation transfer electron paramagnetic resonance spectroscopy (EPR and ST EPR) was used to study the orientation of probe molecules in muscle fibers in different intermediate states of the ATP hydrolysis cycle. A separate procedure was used to obtain ST EPR spectra with precise phase settings even in the case of samples with low spectral intensity. Fibers prepared from rabbit psoas muscle were labeled with isothiocyanate spin labels at the reactive thiol sites of the catalytic domain of myosin | Eur. J. Biochem. 269 2168-2177 2002 FEBS 2002 doi Effect of adenosine 5 - p Ỵ-imido triphosphate on myosin head domain movements Saturation transfer EPR measurements without low-power phase setting Nora Hartvig1 Denes Lorinczy2 Nelli Farkas1 and Joseph Belagyi1 1 Central Research Laboratory and 2Institute of Biophysics School of Medicine University of Pecs Hungary Conventional and saturation transfer electron paramagnetic resonance spectroscopy EPR and ST EPR was used to study the orientation of probe molecules in muscle fibers in different intermediate states of the ATP hydrolysis cycle. A separate procedure was used to obtain ST EPR spectra with precise phase settings even in the case of samples with low spectral intensity. Fibers prepared from rabbit psoas muscle were labeled with isothiocyanate spin labels at the reactive thiol sites of the catalytic domain of myosin. In comparison with rigor a significant difference was detected in the orientation dependence of spin labels in the ADP and adenosine 5 - P y-imido triphosphate AdoPP CH2 P states indicating changes in the internal dynamics and domain orientation of myosin. In the AdoPP CH2 P state approximately half of the myosin heads reflected the motional state of ADP-myosin and the other half showed a different dynamic state with greater mobility. Keywords adenosine 5 - P y-imido triphosphate AdoPP- CH2 P myosin saturation transfer EPR spin-labeling. It is generally accepted that domain movements in the myosin head play a decisive role in the energy-transduction process of muscle contraction 1-5 . It is a multistep process which can produce several conformational states of myosin 6-9 . Extensive studies using different techniques have indicated that the nucleotide-binding pocket does not experience large conformational changes during the hydrolytic cycle 10-12 . However small conformational changes induced by nucleotides in the motor domain should be converted into larger .

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