X-ray Diffraction of Muscle labelled with Antibody to Troponin-C

Rome, Elizabeth; Hirabayashi, Tamio; Perry, S. V.

doi:10.1038/newbio244154a0

Cited by 49 publications

(26 citation statements)

References 18 publications

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“…These values are indistinguishable from those measured by X-ray methods (Rome et al, 1973;Haselgrove, 1975). They imply that neither shrinkage nor elongation influenced the results in any significant way.…”

Section: Resultscontrasting

confidence: 39%

“…The value of this repeat has been measured by X-ray diffraction in unfixed, shrinkagefree specimens (Rome et al, 1973). Thin filament length could thus be computed by multiplying the shrinkagefree spacing by the number of repeats seen in electron micrographs, an approach used earlier (Page & Huxley, I963;Huxley, 1980).…”

Section: Resultsmentioning

confidence: 99%

“…The I-segment contained 22 labelled periods on each side of the Z-line. Multiplying the 44 repeats by either 38.3 nm (Rome et al, 1973; for anti-troponin-C-labelled fibres) or 38.9 run (Haselgrove, 1975; for natural I-band periodicity), gives 1.69 I-tin or 1.7I Jim, respectively. To these values should be added 268 run (0.27 lxm), the length of the naked zone included around the Z-line.…”

Section: Resultsmentioning

confidence: 99%

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Filament lengths in frog semitendinosus and tibialis anterior muscle fibres

Trombitás¹,

Frey

Pollack

1993

J Muscle Res Cell Motil

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In frog semitendinosus muscle the descending limb of the length-tension curve is shifted rightward relative to that of tibialis anterior. Both the plateau right corner and the zero-force intercept are equally shifted. To investigate the reason for this shift, we compared filament lengths in the two muscles. Single fibres were mechanically skinned, stretched to reveal filaments clearly, incubated in a solution containing one of several antibodies to enhance filament visualization, and examined by electron microscopy. We found no differences of filament length. Thick filament lengths were 1.62 and 1.61 microns, respectively. I-segment lengths were measured by two methods. With the first, filament length was the same for both muscles, 1.95 or 1.98 microns, depending on the value taken for the troponin repeat; with the second it was 1.92 and 1.94 microns, respectively, for the two muscles. These differences are insignificant. Thus, the reported differences of shape of the length-tension curve are not explainable in terms of differences of filament length.

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Section: Resultscontrasting

confidence: 39%

Section: Resultsmentioning

confidence: 99%

Section: Resultsmentioning

confidence: 99%

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Filament lengths in frog semitendinosus and tibialis anterior muscle fibres

Trombitás¹,

Frey

Pollack

1993

J Muscle Res Cell Motil

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“…Of these, a pair of reflections at 44.2 and 41.8 nm that have been associated to the protein C (Rome et al 1973a), which binds to the myosin filament with a function still to be fully clarified (Moos et al 1975;Moos and Feng 1980;Squire et al 2003). Another pair of reflections at 38.3 and 39.5 nm likely originating from the troponin repeat along the actin filament (Rome et al 1973b).…”

Section: The Muscle At Restmentioning

confidence: 99%

“…For instance, the doublet at 39.5 and 38.3 nm originates from the actin filament (Huxley and Brown 1967), and has been later attributed to the repeat of troponin along the filament axis (Rome et al 1973b), which gives rise to a reflection sampled by interference effects across the Z line. The doublet at 44.2 and 41.8 nm has been associated with the periodicity of C-protein (Rome 1973a), which lies close to the central region of the thick filament.…”

Section: Origin Of the Fine Structurementioning

confidence: 99%

Recent improvements in small angle x-ray diffraction for the study of muscle physiology

Reconditi¹

2006

Rep. Prog. Phys.

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The molecular mechanism of muscle contraction is one of the most important unresolved problems in Biology and Biophysics. Notwithstanding the great advances of recent years, it is not yet known in detail how the molecular motor in muscle, the class II myosin, converts the free energy of ATP hydrolysis into work by interacting with its track, the actin filament, neither it is understood how the high efficiency in energy conversion depends on the cooperative action of myosin motors working in parallel along the actin filament. Researches in muscle contraction imply the combination of mechanical, biochemical and structural methods in studies that span from tissue to single molecule. Therefore, more than for any other research field, progresses in the comprehension of muscle contraction at molecular level are related to, and in turn contribute to, the advancement of methods in Biophysics.This review will focus on the progresses achieved by time resolved small angle X-ray scattering (SAXS) from muscle, an approach made possible by the highly ordered arrangement of both the contractile proteins myosin and actin in the ca 2 μm long structural unit the sarcomere that repeats along the whole length of the muscle cell. Among the time resolved structural techniques, SAXS has proved to be the most powerful method of investigation, as it allows the molecular motor to be studied in situ, in intact single muscle cells, where it is possible to combine the structural study with fast mechanical methods that synchronize the action of the molecular motors. The latest development of this technique allows Angstrom-scale measurements of the axial movement of the motors that pull the actin filament toward the centre of the sarcomere, by exploiting the X-ray interference between the two arrays of myosin motors in the two halves of the sarcomere.

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Immunological Techniques in Fluorescence and Electron Microscopy Applied to Skeletal Muscle Fibers

Pepe

1983

Comprehensive Physiology

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X-ray Diffraction of Muscle labelled with Antibody to Troponin-C

Cited by 49 publications

References 18 publications

Filament lengths in frog semitendinosus and tibialis anterior muscle fibres

Filament lengths in frog semitendinosus and tibialis anterior muscle fibres

Recent improvements in small angle x-ray diffraction for the study of muscle physiology

Immunological Techniques in Fluorescence and Electron Microscopy Applied to Skeletal Muscle Fibers

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