Flexibility of actin filaments derived from thermal fluctuations. Effect of bound nucleotide, phalloidin, and muscle regulatory proteins

Single actin filaments undergoing brownian movement in two dimensions were observed at 20 degrees C in fluorescence optical video microscopy. The persistence length (Lp) was derived from the analysis of either the cosine correlation function or the average transverse fluctuations of a series of reco...

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Veröffentlicht in:	The Journal of biological chemistry 1995-05, Vol.270 (19), p.11437-11444
Hauptverfasser:	Isambert, H, Venier, P, Maggs, A C, Fattoum, A, Kassab, R, Pantaloni, D, Carlier, M F
Format:	Artikel
Sprache:	eng
Schlagworte:	Actin Cytoskeleton - ultrastructure Actins - chemistry Actins - isolation & purification Actins - metabolism Adenosine Diphosphate - metabolism Adenosine Diphosphate - pharmacology Adenosine Triphosphate - metabolism Adenosine Triphosphate - pharmacology Animals Calmodulin-Binding Proteins - metabolism Hot Temperature Life Sciences Microscopy, Fluorescence Muscle, Skeletal - metabolism Phalloidine - pharmacology Protein Conformation Rabbits Thermodynamics Tropomyosin - metabolism Troponin - metabolism X-Ray Diffraction
Online-Zugang:	Volltext
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