title: Saturation transfer electron paramagnetic resonance study of the mobility of myosin heads in myofibrils under conditions of partial dissociation.
abstract: The rotational motion of rigidly spin-labeled myosin heads of glycerinated myofibrils as reflected in saturation-transfer EPR spectra behaves to a first approximation as though the heads consist of two populations with different rotational motions. An immobilized fraction has a correlation time (tau 2) of approximately 0.5 ms, comparable to that of spin-labeled subfragment-1 (S1) bound to thin filaments, while a mobile fraction has a tau 2 of 10 microseconds, comparable to that of the heads of purified myosin filaments. The effects of nonhydrolyzable ATP analogues, potassium pyrophosphate (PPi), or adenylyl imidodiphosphate, Ca2+, temperature, or ionic strength on the spectra can be analyzed in terms of the fraction of myosin heads immobilized by attachment to thin filaments, without requiring changes in the motion of either attached or detached heads.
mesh_terms: D000266:Adenylyl Imidodiphosphate / Q000494:pharmacology; D000818:Animals; D011756:Diphosphates / Q000494:pharmacology; D004578:Electron Spin Resonance Spectroscopy / Q000379:methods; D007700:Kinetics; D009132:Muscles / Q000648:ultrastructure; D009210:Myofibrils / Q000648:ultrastructure*; D015879:Myosin Subfragments; D009218:Myosins / Q000378:metabolism*; D009994:Osmolar Concentration; D010446:Peptide Fragments / Q000378:metabolism; D011189:Potassium Chloride / Q000494:pharmacology; D011817:Rabbits; D013816:Thermodynamics
chemical_list: D011756:Diphosphates; D015879:Myosin Subfragments; D010446:Peptide Fragments; D000266:Adenylyl Imidodiphosphate; D011189:Potassium Chloride; D009218:Myosins