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- W2155838725 abstract "Point mutations R167H and K168E in tropomyosin Tpm1.1 (TM) disturb Ca2+-dependent regulation of the actomyosin ATPase. To understand mechanisms of this defect we studied multistep changes in mobility and spatial arrangement of tropomyosin, actin and myosin heads during the ATPase cycle in reconstituted ghost fibres using the polarized fluorescence microscopy. It was found that both mutations disturbed the mode of troponin operation in the fibres. At high Ca2+, troponin increased the fraction of actin monomers that were in the “switched on” state, but both mutant tropomyosins were shifted toward the outer actin domains, which decreased the fraction of strongly bound myosin heads throughout the ATPase cycle. At low Ca2+, the R167H-TM was located close to the outer actin domains, which reduced the number of strongly-bound myosin heads. However, under these conditions troponin increased the number of actin monomers that were switched on. The K168E-TM was displaced far to the outer actin domains and troponin binding decreased the fraction of switched on actin monomers, but the proportion of the strongly bound myosin heads was abnormally high. Thus, the mutations differently disturbed transmission of conformational changes between troponin, tropomyosin and actin, which is essential for the Са2+-dependent regulation of the thin filament." @default.
- W2155838725 created "2016-06-24" @default.
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- W2155838725 date "2004-06-01" @default.
- W2155838725 modified "2023-09-25" @default.
- W2155838725 title "339-THE DEVELOPMENT OF NATIONAL SYSTEMS OF HEALTHCARE IN THE EU-MEMBER STATES AND POTENTIAL CONSEQUENCES FOR PSYCHOSOMATIC CARE" @default.
- W2155838725 doi "https://doi.org/10.1016/j.jpsychores.2004.04.075" @default.
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