The use of synchrotron radiation in time-resolved X-ray diffraction studies of myosin layer-line reflections during muscle contraction

Huxley, H. E.; Faruqi, A.R.; Bordas, J.; Koch, Michel H. J.; Milch, James R.

doi:10.1038/284140a0

Cited by 156 publications

(55 citation statements)

References 18 publications

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“…In the case of the equatorial reflections, some specimens showed a transient small increase ofthe [11] intensity by about 10% during release followed by a fall, whereas others showed virtually no change or a small decrease. Some muscles showed a small decrease in the [10] intensity at the time of the quick release, others virtually no change at all. The only conclusion that we can draw at present is that no very large change in the equatorial pattern occurs upon quick release or quick stretch.…”

Section: Resultsmentioning

confidence: 99%

“…The camera and counting system are described in greater detail elsewhere (10)(11)(12). The total flux entering the counter was usually of the order of 1-2 x 105 counts/s.…”

Section: Methodsmentioning

confidence: 99%

“…We have used the electron-positron storage ring DORIS at Deutsches Elektronen Synchrotron -(DESY), Hamburg, as a high-intensity x-ray source, and we have already reported experiments on muscles during normal isometric contraction (10). Improved design of the mirror-monochromator type x-ray camera and of the data recording system has now enabled us to record many of the principal low-angle x-ray reflections from muscle with a time resolution of 1 ms or less.…”

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confidence: 99%

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Millisecond time-resolved changes in x-ray reflections from contracting muscle during rapid mechanical transients, recorded using synchrotron radiation.

Huxley¹,

Simmons²,

Faruqi³

et al. 1981

Proc. Natl. Acad. Sci. U.S.A.

126

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Low-angle x-ray diffraction diagrams have been recorded from frog sartorius muscles by using synchrotron radiation as a high-intensity x-ray source. This has enabled changes in some of the principal reflections of interest to be followed with a time resolution of 1ims, during small but very rapid length changes imposed on a contracting muscle. The 143-A meridional reflection, which is believed to arise from a repeating pattern ofmyosin crossbridges along the length of the muscle, shows large changes in intensity in these circumstances. During both rapid releases and rapid stretches, by amounts that produce a translation ofactin and myosin filaments past each other by about 100 A and that are completed in about a millisecond (i.e., before significant cross-bridge detachment would be expected), an almost synchronous decrease in 143-A intensity occurs, by 50% or more. This is followed, in the case ofquick releases, by a rapid partial recovery of intensity lasting 5-6 ms (which may represent cross-bridge release and reattachment) and then by a more gradual return to the normal isometric value. Quick stretches show only the slower return of intensity. Immediately after the length change, the initial drop in 143-A intensity can be reversed if the release-(or stretch) is reversed. These changes provide evidence ofa more direct kind than has hitherto been available that the active sliding ofactin filaments past myosin filaments during contraction is produced by longitudinal movement of attached cross-bridges.The outstanding problem in understanding the mechanism of muscular contraction is to discover the nature of the process by which the relative sliding force between actin and myosin filaments is developed. It is generally supposed that the crossbridges, the enzymatically active heads of the myosin molecules, function in a cyclical manner to produce this force. It is thought that they attach to actin in one part of their cycle, then undergo some structural change that enables them to exert tension and, during shortening, to pull the actin along a short distance-probably 100 A or so-towards the center ofthe A-band. They then detach from actin and are recharged by ATP before beginning a new cycle of attachment further out along the actin filament (1, 2). Whilst this general mechanism has been able to give a good account of many phenomena in muscle, it has proved remarkably difficult to produce direct and decisive evidence that the cross-bridges really do behave in this fashion, because of. the inherent difficulty of obtaining dynamic structural information on the size and time scales involved. Moreover, because the processes take place asynchronously at all the cross-bridges, probes of their configuration will usually give only an averaged value of changes in them during the cycle.Surviving muscles give low-angle x-ray diffraction diagrams that contain a considerable amount of information about.-the configuration ofthe cross-bridges and that alter incharacteristic ways during contraction (3-7). The changes in t...

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Section: Resultsmentioning

confidence: 99%

“…The camera and counting system are described in greater detail elsewhere (10)(11)(12). The total flux entering the counter was usually of the order of 1-2 x 105 counts/s.…”

Section: Methodsmentioning

confidence: 99%

mentioning

confidence: 99%

See 1 more Smart Citation

Millisecond time-resolved changes in x-ray reflections from contracting muscle during rapid mechanical transients, recorded using synchrotron radiation.

Huxley¹,

Simmons²,

Faruqi³

et al. 1981

Proc. Natl. Acad. Sci. U.S.A.

126

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“…At about that time Gabriel and Dupont [35] developed a position sensitive electronic detector, another major requirement for time-resolved experiments. But not until the end of the seventies, the first real-time X-ray experiments on muscle using a twodimensional TV detector became feasible [20].…”

Section: G Rappmentioning

confidence: 99%

“…[20] or for review [21]). More recently, Cecchi et al [22] extended this approach to work on single muscle fibres only 100 μm in diameter.…”

Section: Trigger Mechanismsmentioning

confidence: 99%

Time-Resolved X-Ray Diffraction Studies on Biological Systems

Rapp¹

1992

Acta Phys. Pol. A

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Understanding of biological function requires knowledge both on structural and dynamical aspects. The aim of time-resolved X-ray diffraction is to combine structural and kinetic methods by monitoring structural or conformational changes within a single protein or assemblies of proteins during their biological action in real time. This requires (i) a powerful X-ray source, (ii) appropriate detectors capable of dealing with high local and total count rates and (iii) a suitable trigger mechanism. These aspects are briefly discussed with emphasis on light as trigger for initiation of structural or conformational changes. Examples are presented on muscle contraction, lipid• phase transitions, the photocycle of bacteriorhodopsin and the application of Laue crystallography on the protein p21.

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

Pollard

Goldman

2013

Cytoskeleton

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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.

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The use of synchrotron radiation in time-resolved X-ray diffraction studies of myosin layer-line reflections during muscle contraction

Cited by 156 publications

References 18 publications

Millisecond time-resolved changes in x-ray reflections from contracting muscle during rapid mechanical transients, recorded using synchrotron radiation.

Millisecond time-resolved changes in x-ray reflections from contracting muscle during rapid mechanical transients, recorded using synchrotron radiation.

Time-Resolved X-Ray Diffraction Studies on Biological Systems

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

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