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Special Issue "Advances in Muscle Contraction Studies"

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A special issue of International Journal of Molecular Sciences (ISSN 1422-0067). This special issue belongs to the section "Biochemistry, Molecular Biology and Biophysics".

Deadline for manuscript submissions: closed (31 October 2010)

Special Issue Editor

Guest Editor
Prof. Dr. Mark L. Richter (Website)

Molecular Biosciences, Haworth Hall, Room 4031, 1200 Sunnyside Avenue, Lawrence, KS 66045-7534, USA
Interests: ATP hydrolysis-driven motor proteins; biochemical and biophysical approaches to examining mechanisms by which protein-protein interactions lead to large conformational changes resulting in translational or rotational motion; structure and function of the photosynthetic F1-ATPase motor protein

Keywords

  • muscle contraction mechanism
  • models
  • motor proteins
  • cell motility
  • actin-myosin ATPase
  • physical chemistry of water; water solitons
  • hydraulic compression
  • ATP hydrolysis
  • cytoplasm steaming
  • bioenergetics
  • proton-motive-force
  • Brownian motor
  • actin motors
  • microtubule motors
  • plant specific motors
  • transport of proteins and vesicles
  • RNA polymerase
  • topoisomerases
  • Fokker-Planck equation
  • Monte Carlo method
  • molecular dynamics
  • brownian motor
  • FRET
  • electrophysiology
  • optical tweezers
  • magnetic tweezers
  • locomotion

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Published Papers (3 papers)

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Research

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Open AccessArticle Geometrical Conditions Indispensable for Muscle Contraction
Int. J. Mol. Sci. 2011, 12(4), 2138-2157; doi:10.3390/ijms12042138
Received: 22 February 2011 / Revised: 10 March 2011 / Accepted: 18 March 2011 / Published: 29 March 2011
Cited by 1 | PDF Full-text (2275 KB) | HTML Full-text | XML Full-text
Abstract
Computer simulation has uncovered the geometrical conditions under which the vertebrate striated muscle sarcomere can contract. First, all thick filaments should have identical structure, namely: three myosin cross-bridges, building a crown, should be aligned at angles of 0°, 120°, 180°, and the [...] Read more.
Computer simulation has uncovered the geometrical conditions under which the vertebrate striated muscle sarcomere can contract. First, all thick filaments should have identical structure, namely: three myosin cross-bridges, building a crown, should be aligned at angles of 0°, 120°, 180°, and the successive crowns and the two filament halves should be turned around 120°. Second, all thick filaments should act simultaneously. Third, coordination in action of the myosin cross-bridges should exist, namely: the three cross-bridges of a crown should act simultaneously and the cross-bridge crowns axially 43 and 14.333 nm apart should act, respectively, simultaneously and with a phase shift. Fifth, six thin filaments surrounding the thick filament should be turned around 180° to each other in each sarcomere half. Sixth, thin filaments should be oppositely oriented in relation to the sarcomere middle. Finally, the structure of each of the thin filaments should change in consequence of strong interaction with myosin heads, namely: the axial distance and the angular alignment between neighboring actin monomers should be, respectively, 2.867 nm and 168° instead of 2.75 nm and 166.15°. These conditions ensure the stereo-specific interaction between actin and myosin and good agreement with the data gathered by electron microscopy and X-ray diffraction methods. The results suggest that the force is generated not only by the myosin cross-bridges but also by the thin filaments; the former acts by cyclical unwrapping and wrapping the thick filament backbone, and the latter byelongation. Full article
(This article belongs to the Special Issue Advances in Muscle Contraction Studies)
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Review

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Open AccessReview The Different Muscle-Energetics during Shortening and Stretch
Int. J. Mol. Sci. 2011, 12(5), 2891-2900; doi:10.3390/ijms12052891
Received: 21 February 2011 / Revised: 17 March 2011 / Accepted: 12 April 2011 / Published: 3 May 2011
Cited by 3 | PDF Full-text (125 KB) | HTML Full-text | XML Full-text
Abstract
The helical shape of the thin filaments causes their passive counterclockwise rotation during muscle stretch that increases tensile stress and torque at first by unwinding and then by winding up the four anchoring Z-filaments. This means storage of energy in the series [...] Read more.
The helical shape of the thin filaments causes their passive counterclockwise rotation during muscle stretch that increases tensile stress and torque at first by unwinding and then by winding up the four anchoring Z-filaments. This means storage of energy in the series elastic Z-filaments and a considerable decrease of the liberated energy of heat and work to (h—wap), where h is the heat energy and wap the stretch energy induced from outside by an apparatus. The steep thin filament helix with an inclination angle of 70° promotes the passive rotation during stretch, but impedes the smooth sliding of shortening by increased friction and production of frictional heat. The frictional heat may be produced by the contact with the myosin cross-bridges: (1) when they passively snap on drilling thin filaments from cleft to cleft over a distance 2 × 2.7 nm = 5.4 nm between the globular actin monomers in one groove, causing stepwise motion; or (2) when they passively cycle from one helical groove to the next (distance 36 nm). The latter causes more heat and may take place on rotating thin filaments without an effective forward drilling (“idle rotation”), e.g., when they produce “unexplained heat” at the beginning of an isometric tetanus. In an Appendix to this paper the different states of muscle are defined. The function of its most important components is described and rotation model and power-stroke model of muscular contraction is compared. Full article
(This article belongs to the Special Issue Advances in Muscle Contraction Studies)
Open AccessReview The Role of Alpha-Dystrobrevin in Striated Muscle
Int. J. Mol. Sci. 2011, 12(3), 1660-1671; doi:10.3390/ijms12031660
Received: 16 December 2010 / Revised: 29 January 2011 / Accepted: 23 February 2011 / Published: 4 March 2011
Cited by 8 | PDF Full-text (329 KB) | HTML Full-text | XML Full-text
Abstract
Muscular dystrophies are a group of diseases that primarily affect striated muscle and are characterized by the progressive loss of muscle strength and integrity. Major forms of muscular dystrophies are caused by the abnormalities of the dystrophin glycoprotein complex (DGC) that plays [...] Read more.
Muscular dystrophies are a group of diseases that primarily affect striated muscle and are characterized by the progressive loss of muscle strength and integrity. Major forms of muscular dystrophies are caused by the abnormalities of the dystrophin glycoprotein complex (DGC) that plays crucial roles as a structural unit and scaffolds for signaling molecules at the sarcolemma. α-Dystrobrevin is a component of the DGC and directly associates with dystrophin. α-Dystrobrevin also binds to intermediate filaments as well as syntrophin, a modular adaptor protein thought to be involved in signaling. Although no muscular dystrophy has been associated within mutations of the α-dystrobrevin gene, emerging findings suggest potential significance of α-dystrobrevin in striated muscle. This review addresses the functional role of α-dystrobrevin in muscle as well as its possible implication for muscular dystrophy. Full article
(This article belongs to the Special Issue Advances in Muscle Contraction Studies)

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