Electron microscope studies on the structure of natural and synthetic protein filaments from striated muscle

Huxley, H. E.

doi:10.1016/s0022-2836(63)80008-x

Cited by 1,391 publications

(416 citation statements)

References 36 publications

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“…Although we, along with others, have previously provided details about the ultrastructural arrangement of myosin in the thick filaments from frogs (Cantino & Squire, 1986;, 1993Craig et al, 1992;Levine, 1993), fish (VarrianoMarston et al, 1984;Kensler & Stewart, 1989) and rabbits (Huxley, 1963;Craig & Offer, 1976;Trinick & Elliott, 1979;Ip & Heuser, 1983;Starr et al, 1985;Bennett et al, 1986;Menetret et al, 1990;Kensler & Stewart, 1993), the structure of the chicken thick filament has remained relatively unknown. In this study we have demonstrated that the arrangement of the myosin heads on the chicken thick filament is temperature-dependent and have also provided evidence that these filaments have a three-stranded arrangement of the cross-bridges.…”

Section: Discussionmentioning

confidence: 87%

The chicken muscle thick filament: temperature and the relaxed cross-bridge arrangement

Kensler

Woodhead

1995

J Muscle Res Cell Motil

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Although chicken myosin S1 has recently been crystallized and its structure analysed, the relaxed periodic arrangement of myosin heads on the chicken thick filament has not been determined. We report here that the cross-bridge array of chicken filaments is temperature sensitive, and the myosin heads become disordered at temperatures near 4 degrees C. At 25 degrees C, however, thick filaments from chicken pectoralis muscle can be isolated with a well ordered, near-helical, arrangement of cross-bridges as seen in negatively stained preparations. This periodicity is confirmed by optical diffraction and computed transforms of images of the filaments. These show a strong series of layer lines near the orders of a 43 nm near-helical periodicity as expected from X-ray diffraction. Both analysis of phases on the first layer line, and computer filtered images of the filaments, are consistent with a three-stranded arrangement of the myosin heads on the filament.

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Section: Discussionmentioning

confidence: 87%

The chicken muscle thick filament: temperature and the relaxed cross-bridge arrangement

Kensler

Woodhead

1995

J Muscle Res Cell Motil

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“…Many reports showed that myosin heads are angled when they bind to actin filaments in the rigor state (Huxley, 1963;Reedy et al, 1965). In the three-dimensional reconstruction of actin filaments decorated with $1, the angle of $1 was close to 90 ° with the filament axis in the region near the thin filament and smaller than 45 ° in the tail region (Toyoshima & Wakabayashi, 1985;Milligan & Flicker, 1987).…”

Section: Angles Of the Crossbridgesmentioning

confidence: 99%

Structural change of crossbridges of rabbit skeletal muscle during isometric contraction

Hirose

Wakabayashi

1993

J Muscle Res Cell Motil

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Structural changes of crossbridges during isometric contraction have been studied by electron microscopy. Chemically skinned rabbit fibres were rapidly frozen either in activating solution or in ATP-free (rigor) solution, freeze-substituted and embedded. Longitudinal sections of muscle fibres show that the number of crossbridges in active fibres (isometric contraction) is approximately the same as in rigor fibres. Crossbridges of the active and rigor states differ in their shapes, angles and manner of arrangement on the thin filaments. In rigor many crossbridges are wide near the thin filaments and narrow near the thick filament shafts; in active fibres they have more uniform width along their length. The angle of the crossbridges in active fibres is somewhat variable. The average angle is approximately 90 degrees to the filament axis. The crossbridges are arranged on the thin filament retaining the 14.3 nm thick filament periodicity. The crossbridges in rigor are tilted and their arrangement near the thin filament reveals the 36 nm actin periodicity. The variability in the shapes of the crossbridges in active fibres is still higher when we look at them in cross-sections of muscle fibres. The crossbridge shapes in the cross-sections were classified and the relative frequency of different shapes was determined. The shapes that are commonly observed in active fibres are similar in that the majority of the mass of the crossbridges is farther away from the thin filament than the crossbridges in rigor fibres.

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“…The rod region of myosin plays a significant role in the formation of the myosin filament [10], and myosin molecules aggregate and assemble into insoluble filaments when they exist in a low-ionic-strength medium and at neutral pH. Figure 30.3 shows the solubility change in myosin and its subfragments as a result of glycosylation [12].…”

Section: Molecular Mechanism Of Water Solubilisation By Glycosylationmentioning

confidence: 99%

A New Approach to the Functional Improvement of Fish Meat Proteins

Saeki

2010

Handbook of Seafood Quality, Safety and Health Applications

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Fish and shellfish are important protein sources and are widely used as raw material for preparation of processed seafood. Fish meat is highly nutritious, and its myofibrillar (Mf) protein has excellent functional properties, such as emulsion-and gel-forming abilities, and water-holding capabilities. Various technologies for dealing with fish meat, such as freezedrying, spray-drying, extrusion cooking, and high-hydrostatic-pressure processing, have been developed and applied to the seafood industry. However, fish Mf protein is thermally and chemically less stable than that of other vertebrates, and the food functionality is impaired easily as protein denaturation progresses. Therefore, the suppression of protein denaturation during the storage of materials and food processing is important to the manufacturing of high-quality processed seafood. Processing technologies, such as low-temperature storage to keep fish flesh close to freezing (partial freezing), mixing with edible cryoprotectants, and rapid neutralisation of meat by washing with alkaline solution, have been developed for decreasing protein denaturation during processing.Protein glycosylation is an effective method for improving the functional properties of proteins, and various techniques are available to prepare synthetic glycoproteins [3][4][5]8,18]. Recently, the focus has been placed on the neoglycoprotein-synthetic system using the Maillard reaction [14] as an effective method to improve the functional properties of food proteins. The protein glycosylation system is superior to other types of chemical modification for food proteins because it proceeds under mild and safe conditions without the use of chemicals. Food proteins, such as ovalbumin [14], ␤-lactoglobulin [9], phosvitin [26], lysozyme [36], and protamine [21], have been conjugated with various reducing sugars through the Maillard reaction to improve their functional properties such as thermal stability, emulsion-forming ability, antioxidant system to fish meat protein, and succeeded in improving its food functionality. This chapter reviews the enhancing effect of glycosylation through the Maillard reaction on food functionality of fish muscle protein and provides a discussion on the feasibility of using the protein glycosylation technology in the seafood industry. Handbook of Seafood Q uality, Safety and Health ApplicationsEdited by Cesarettin Alasalvar, Fereidoon Shahidi, Kazuo Miyashita and Udaya Wanasundara

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Electron microscope studies on the structure of natural and synthetic protein filaments from striated muscle

Cited by 1,391 publications

References 36 publications

The chicken muscle thick filament: temperature and the relaxed cross-bridge arrangement

The chicken muscle thick filament: temperature and the relaxed cross-bridge arrangement

Structural change of crossbridges of rabbit skeletal muscle during isometric contraction

A New Approach to the Functional Improvement of Fish Meat Proteins

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