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X-ray diffraction evidence for myosin-troponin connections and tropomyosin movement during stretch activation of insect flight muscle
TLDR
The time-resolved sequence of molecular changes suggests a mechanism for stretch activation, in which troponin bridges mechanically tug tropomyosin aside to relieve tropomyOSin’s steric blocking of myosin–actin binding, which enables subsequent force production. Expand
Reverse actin sliding triggers strong myosin binding that moves tropomyosin
Actin/myosin interactions in vertebrate striated muscles are believed to be regulated by the “steric blocking” mechanism whereby the binding of calcium to the troponin complex allows tropomyosin (TM)Expand
Similarities and differences between frozen-hydrated, rigor acto-S1 complexes of insect flight and chicken skeletal muscles.
TLDR
These are the first unconstrained models of IFM S1 bound to actin and the first direct comparison of the vertebrate and invertebrate skeletal myosin II classes, the latter for which, data on the structure of discrete acto-S1 complexes, are not readily available. Expand
X-Ray Diffraction “Movie” Of Complete Oscillatory Work Cycles Myogenically Produced In Glycerinated Insect Flight Muscle (IFM)
When slightly calcium-activated (pCa ∼5.7, gives ∼0.2 peak isometric force), glycerinated Lethocerus insect flight muscle (IFM) can be mechanically stretch-activated at constant [Ca2+] to give aExpand
Platform U: Muscle: Fiber & Molecular Mechanics & Structure
showed that although local, near-to-equilibrium systems may be interlocked.Thus, for example, if the act of proton pumping were reversibly connected toATP synthesis, the ATP could then be used as aExpand