Cross-bridge conformation as revealed by x-ray diffraction studies on insect flight muscles with ATP analogues.
The effects of three ATP analogues, alpha,beta-methylene-ATP [ATP(alpha,beta-CH1)], adenosine 5'-0-(3-thiotrophosphate) [ATP(gamma-S)], and beta,gamma-amino-ATP [ATP(beta,gamma-NH)] at various concentrations and temperatures on the X-ray fiber diagrams of glycerinated flight muscles from a water bug (Lethocerus maximus) have been investigated. It is shown that the "relaxed" state can be obtained with all three analogues at high concentrations, the result being particularly clear with ATP(gamma-S). It is inferred that the binding of an ATP-like molecule suffices to produce the relaxed state. At low concentrations ATP(beta,gamma-NH) produces state intermediate between rigor and relaxed which is not simply a mixture of the two. The possible nature of the intermediate is discussed.
D000199:Actins; D000205:Actomyosin; D000255:Adenosine Triphosphate / Q000031:analogs & derivatives*; D000818:Animals; D001665:Binding Sites; D005426:Flight, Animal; D005990:Glycerol; D007313:Insecta; D007700:Kinetics; D008433:Mathematics; D009132:Muscles / Q000648:ultrastructure*; D009218:Myosins; D011485:Protein Binding; D011487:Protein Conformation; D013696:Temperature; D014961:X-Ray Diffraction
D000199:Actins; D000255:Adenosine Triphosphate; D000205:Actomyosin; D009218:Myosins; D005990:Glycerol