On the molecular basis for chemomechanical energy transduction in muscle.
Herein it is developed that energy transduction in muscle is an activity of myosin S-1 and its ligands, actin (A) and nucleotide (N). S-1 shares with other molecular particles (e.g., hemoglobin) the property that binding events at one of its sites, the N-site, influences binding events at a remote site, the A site (specifically, influences both the actin affinity and actin attachment angle at the A site). However, there is a crucial difference between S-1 and the better-known systems. Because the N site is enzymatic, it has a temporal sequence of occupants; this imposes a temporal sequence of actin attitudes--i.e., a sequence of mechanical events.
D000199:Actins / Q000502:physiology*; D000255:Adenosine Triphosphate / Q000378:metabolism; D055592:Biophysical Phenomena; D001703:Biophysics; D007700:Kinetics; D008954:Models, Biological; D009119:Muscle Contraction; D009218:Myosins / Q000502:physiology*; D011487:Protein Conformation
D000199:Actins; D000255:Adenosine Triphosphate; D009218:Myosins