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FT-Raman studies on the transformation of G-actin to F-actin, the binding of cisplatin and transplatin to F-actin and the effects of the conformation of F-actin

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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Dynamics of F‐actin and F‐actin/filamin networks as studied by photon correlation spectroscopy

Biopolymers, 1990
AbstractPhoton 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, 1992
The 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, 1977
The 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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Interaction of F-actin with troponin constituents

Biochimica et Biophysica Acta (BBA) - Protein Structure, 1973
Abstract 1. 1.|Interaction of F-actin with troponin and its constituents has been studied. F-Actin is precipitated only by preparations of troponin which contain a high ratio of the 39 000 daltons component (TN-T) to the 19 000 daltons component (TN-C).
W, Drabikowski, E, Nowak
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The multiple links between actin and mitochondria

Nature Reviews Molecular Cell Biology, 2023
Tak Shun Fung   +2 more
exaly  

Biochemical and mechanical regulation of actin dynamics

Nature Reviews Molecular Cell Biology, 2022
Pekka Lappalainen   +2 more
exaly  

A Discourse on Modeling F-Actin

Journal of Structural Biology, 1995
C E, Schutt   +3 more
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