Does myosin-substrate interaction in vitro result in a delocalized conformation change?
The effect of substrate on the far UV (185-250 nm) and near UV (250-325 nm) circular dichroism (CD) of myosin and heavy meromyosin (HMM) was studied. The following results were obtained with the addition of ATP (during various conditions of hydrolysis), ADP, and pyrophosphate: (1) no changes were observed in the far UV CD, (2) ATP and ADP perturbed the near UV CD only at spectral regions below 280 nm coinciding with the regions of their optical activity, (3) the optically inactive pyrophosphate caused no change in the near UV CD, and (4) myosin and HMM gave exactly the same results. These results suggest that myosin-substrate interaction in vitro does not result in a delocalized conformational change.
D000244:Adenosine Diphosphate / Q000378:metabolism / Q000494:pharmacology*; D000251:Adenosine Triphosphatases / Q000378:metabolism; D000255:Adenosine Triphosphate / Q000378:metabolism / Q000494:pharmacology*; D000818:Animals; D001665:Binding Sites; D002942:Circular Dichroism; D011756:Diphosphates / Q000378:metabolism / Q000494:pharmacology*; D015879:Myosin Subfragments / Q000378:metabolism; D009218:Myosins / Q000378:metabolism; D009905:Optical Rotatory Dispersion; D011487:Protein Conformation / Q000187:drug effects; D011817:Rabbits
D011756:Diphosphates; D015879:Myosin Subfragments; D000244:Adenosine Diphosphate; D000255:Adenosine Triphosphate; D000251:Adenosine Triphosphatases; D009218:Myosins