Результаты поиска по 'molecular motors':
Найдено статей: 3
  1. Trifonenkov V.P., Kargovsky A.V.
    Cluster models of molecular motors: kinesin and myosin V
    Computer Research and Modeling, 2014, v. 6, no. 5, pp. 747-760

    We present a semiphenomenological model of the two molecular motors: kinesin and myosin V, which play a great role in intracellular transport. The temporal dynamics of changes in the characteristic geometric parameters and the elastic stresses generated during the movement of motors is studied. The rates of movement of kinesin and myosin V, and their dependence on the concentration of ATP are discussed.

    Keywords: molecular motors, myosin V, kinesin.
    Views (last year): 2. Citations: 1 (RSCI).
  2. Pogrebnaya A.F.
    Synthesis of ATP by F1-ATPase in stochastic model
    Computer Research and Modeling, 2009, v. 1, no. 2, pp. 217-223

    The paper continues our series of papers [1-4] devoted to the development of mathematical model on rotation of F1-AТPase molecular motor. Here it has been considered the synthesis of ATP induced by external force applied to the rotor.

    Keywords: ATP, ATPase, external force.
    Views (last year): 2. Citations: 1 (RSCI).
  3. Guleenkova V.D., Ershova D.M., Tsaturyan A.K., Koubassova N.A.
    Molecular dynamics study of the effect of mutations in the tropomyosin molecule on the properties of thin filaments of the heart muscle
    Computer Research and Modeling, 2024, v. 16, no. 2, pp. 513-524

    Muscle contraction is controlled by Ca2+ ions via regulatory proteins, troponin and tropomyosin, associated with thin actin filaments in sarcomeres. Depending on the Ca2+ concentration, the thin filament rearranges so that tropomyosin moves along its surface, opening or closing access to actin for the motor domains of myosin molecules, and causing contraction or relaxation, respectively. Numerous point amino acid substitutions in tropomyosin are known, leading to genetic pathologies — myo- and cardiomyopathies caused by changes in the structural and functional properties of the thin filament. The results of molecular dynamics modeling of a fragment of a thin filament of cardiac muscle sarcomeres formed by fibrillar actin and wildtype tropomyosin or with amino acid substitutions: the double stabilizing substitution D137L/G126R and the cardiomyopathic substitution S215L are presented. For numerical calculations, we used a new model of a thin filament fragment containing 26 actin monomers and 4 tropomyosin dimers, with a refined structure of the region of overlap of neighboring tropomyosin molecules in each of the two tropomyosin strands. The simulation results showed that tropomyosin significantly increases the bending stiffness of the thin filament, as previously found experimentally. The double stabilizing replacement D137L/G126R leads to a further increase in this rigidity, and the replacement S215L, on the contrary, leads to its decrease, which also corresponds to experimental data. At the same time, these substitutions have different effects on the angular mobility of the actin helix and only slightly modulate the angular mobility of tropomyosin cables relative to the actin helix and the population of hydrogen bonds between negatively charged tropomyosin residues and positively charged actin residues. The results of the verification of the new model demonstrate that its quality is sufficient for the numerical study of the effect of single amino acid substitutions on the structure and dynamics of thin filaments and study the effects leading to dysregulation of muscle contraction. This model can be used as a useful tool for elucidating the molecular mechanisms of some genetic diseases and assessing the pathogenicity of newly discovered genetic variants.

    Keywords: cardiac muscle, actin, tropomyosin, molecular dynamics, mutations, cardiomyopathy.

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