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Biomimetic F‐Actin Cortex Models
ChemPhysChem, 2009AbstractSince its first production from muscle tissue more than 65 years ago, our knowledge about actin has come a long way. While at the beginning it was identified as a muscle protein, nowadays actin is considered as one of the most important components of the cytoskeleton, playing a crucial role in cell motility, adhesion, morphology and ...
Haraszti, T., Clemen, A., Spatz, J.
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Journal of Theoretical Biology, 1985
The equipartition theorem is used to calculate the mode amplitudes for F-actin thermal torsion. The amplitudes phi n are found to scale as n-1, (EI)-1/2, and L1/2, where n is mode number, EI is actin bending stiffness, and L is filament length. Depending on conditions, the amplitude can be as large as 15 degrees; this is discussed briefly in terms of ...
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The equipartition theorem is used to calculate the mode amplitudes for F-actin thermal torsion. The amplitudes phi n are found to scale as n-1, (EI)-1/2, and L1/2, where n is mode number, EI is actin bending stiffness, and L is filament length. Depending on conditions, the amplitude can be as large as 15 degrees; this is discussed briefly in terms of ...
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Modeling of the F-Actin Structure
2007Actin has been a major target for structural studies in biology since F. B. Straub discovered it in 1942.1 This is probably because actin is one of the most abundant proteins in the eukaryotic cell as well as a key player in many physiological events, ranging from genetics to motility.
Oda, T. +4 more
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Natural F-actin III. Natural F-actin as inactive polymer
Biochimica et Biophysica Acta (BBA) - Bioenergetics, 1969Abstract 1. 1. Natural F-actin was found to be short in length, and the length distribution was not changed by storage demonstrating that an end-to-end interaction between natural F-actins was lacking. 2. 2. Natural F-actin never accelerated the G-F transformation of Straub G-actin, but a great acceleration was produced by sonic treatment ...
Michiki Kasai, Hiroko Hama
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Current Opinion in Structural Biology, 1998
The study of proteins that bind filamentous actin (F-actin) is entering an exciting stage as more and more structures are determined. After more than 50 years in which the focus was on muscle proteins, emphasis has recently shifted towards understanding the complex interplay among actin-binding molecules in non-muscle cells.
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The study of proteins that bind filamentous actin (F-actin) is entering an exciting stage as more and more structures are determined. After more than 50 years in which the focus was on muscle proteins, emphasis has recently shifted towards understanding the complex interplay among actin-binding molecules in non-muscle cells.
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International Journal of Biological Macromolecules, 1997
The conformation change of G-actin of F-actin and the binding modes of cisplatin and transplatin to F-actin have been studied by FT-Raman spectroscopy. The studies show that the process of polymerization is related to the vibration of C-S Gauche mode (approximately 650 cm-1), which indicates that the methionine (Met) contributes to the polymerization ...
H H, Zeng, Z H, Xu, K, Wang
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The conformation change of G-actin of F-actin and the binding modes of cisplatin and transplatin to F-actin have been studied by FT-Raman spectroscopy. The studies show that the process of polymerization is related to the vibration of C-S Gauche mode (approximately 650 cm-1), which indicates that the methionine (Met) contributes to the polymerization ...
H H, Zeng, Z H, Xu, K, Wang
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Dynamics of F‐actin and F‐actin/filamin networks as studied by photon correlation spectroscopy
Biopolymers, 1990AbstractPhoton correlation spectroscopy was used to study both F‐actin and F‐actin/filamin networks in solution. The measured autocorrelation functions were analyzed with the inverse Laplace transform CONTIN. The resulting frequency distributions consist of maximal five relatively narrow peaks.
J, Seils, B M, Jockusch, T, Dorfmuller
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Instability of F-Actin in the Absence of ATP: A Small Amount of Myosin Destabilizes F-Actin
The Journal of Biochemistry, 1992The effects of the neutral salt concentration, pH, and coexistence of myosin on the denaturation of F-actin without ATP at low temperature were studied using the DNase I inhibition assay. The percent denaturation of F-actin gradually increased with a decrease in pH from 8.0 to 5.2, on incubation for 2 weeks in the presence of 50 mM KCl at 0 degrees C ...
Y, Ikeuchi +4 more
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Electronmicroscopic investigation of the flexibility of f-actin
Biochimica et Biophysica Acta (BBA) - Protein Structure, 1977The contour lenghts and the end-to-end distances of a large number of F-actin filaments were measured in electronmicrographs. Preparation of F-actin for electron-microscopy was made at three different temperatures. The flexibility parameter or the elastic modulus for bending of F-actin was determined from the relation between the contour length and the
T, Takebayashi, Y, Morita, F, Oosawa
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On the elastic properties of tetramethylrhodamine F-actin
Biophysical Chemistry, 2001(Iodoacetamido)tetramethylrhodamine disrupts F-actin. At the 1:1 fluorophore to actin (as monomer) ratio approximately 80% of the protein becomes non-sedimentable. The fluorescent, non-sedimentable actin copolymerizes with G-actin to yield fluorescent filaments.
CINTIO O. +3 more
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