Remembrance of Hugh E. Huxley, a founder of our field

@article{Pollard2013RemembranceOH,
  title={Remembrance of Hugh E. Huxley, a founder of our field},
  author={Thomas D. Pollard and Yale E. Goldman},
  journal={Cytoskeleton},
  year={2013},
  volume={70}
}
Hugh E. Huxley (1924–2013) carried out structural studies by X‐ray fiber diffraction and electron microscopy that established how muscle contracts. Huxley's sliding filament mechanism with an ATPase motor protein taking steps along an actin filament, established the paradigm not only for muscle contraction but also for other motile systems using actin and unconventional myosins, microtubules and dynein and microtubules and kinesin. © 2013 Wiley Periodicals, Inc. 
1 Citations
Hugh E. Huxley: the compleat biophysicist.
TLDR
It is shown how Huxley's life and work, with its focus on a single scientific problem, had impact far beyond the field of muscle contraction to the benefit of multiple fields of cellular and structural biology. Expand

References

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TLDR
Improvements in technology have made it possible to study the fine structure of some of the X-ray reflections from contracting muscle during mechanical transients, and these are currently providing remarkable insights into the detailed mechanism of force development by myosin cross-bridges. Expand
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TLDR
Tropomyosin movement, in response to calcium binding to troponin, is the first structural step in muscular contraction, and is the prerequisite for myosin binding. Expand
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TLDR
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The use of synchrotron radiation in time-resolved X-ray diffraction studies of myosin layer-line reflections during muscle contraction
Experiments on striated muscle have been carried out at the EMBL Outstation at DESY, Hamburg, using the electron–positron storage ring DORIS as a high-intensity X-ray source. The low-angleExpand
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TLDR
Observations of filament extensions totaling 2-3 nm per half-sarcomere may necessitate some significant revision of the interpretation of a number of mechanical experiments in muscle, in which it has usually been assumed that virtually all of the elasticity resides in the cross-bridges. Expand
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TLDR
In the present studies, low-angle X-ray diffraction technique has been used to study the molecular structure of these two proteins, actin and myosin, and their arrangement in living muscle under various conditions. Expand
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TLDR
It is suggested that the linear part ofheavy meromyosin is flexibly attached to the backbone of the thick filaments and to the globular part of heavy meromyOSin (which carries the actin-binding and ATPase sites), so that, by tilting farther outwards, this link can alter the radius at which the active end of the cross-bridge is situated. Expand
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TLDR
The results obtained show that the filaments are structurally polarized, and in muscle are arranged so that all of them attached on one side of a given Z-line point in one direction, whilst those on the other are oppositely oriented. Expand
The low-angle x-ray diagram of vertebrate striated muscle and its behaviour during contraction and rigor.
TLDR
The results indicate that a co-operative re-organization of the helical arrangement of myosin cross-bridges may occur when they bind to the sites on the actin filaments in such a way as to maximize the number of points of near-registration. Expand
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TLDR
Under appropriate conditions (in the absence of Ca2+ and in the presence of pyrophosphate), the structure of the complex of subfragments of myosin with actin was significantly altered by the presenceof tropomyosin-troponin. Expand
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