Abstract:
:The orientation of the myosin neck was monitored using electron paramagnetic resonance (EPR) spectroscopy. Gizzard regulatory light chain was labeled with a nitroxide spin probe and exchanged for the native subunit, located in the myosin neck, in rabbit psoas muscle fibers. The EPR spectra of rigor fibers indicated a substantial degree of probe immobilization and showed a strong dependence on the orientation of the fiber axis relative to the magnetic field, indicating that the neck was ordered in this state. Spectra of relaxed fibers at 24 degrees C showed that the neck was disordered, but the spectra of relaxed fibers at 4 degrees C indicated that the neck was partially ordered. Active fibers at the two temperatures produced spectra identical to relaxed fibers, indicating that no novel angles could be seen in the neck during the powerstroke. Proteolytic fragments of myosin, S1 and HMM, were exchanged with labeled light chains and bound to thin filaments in unlabeled fibers. The distribution of probe orientations for HMM was identical to that of labeled rigor fibers, while S1 showed a slightly different distribution, suggesting that the neck is distorted (by a few degrees) by the interactions of the two heads of myosin when bound to actin.
journal_name
Biochemistryjournal_title
Biochemistryauthors
Zhao L,Gollub J,Cooke Rdoi
10.1021/bi960505vsubject
Has Abstractpub_date
1996-08-06 00:00:00pages
10158-65issue
31eissn
0006-2960issn
1520-4995pii
bi960505vjournal_volume
35pub_type
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