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On the elastic properties of tetramethylrhodamine F-actin
1Dipartimento di Biochimica e Biologia Molecolare, Università di Ferrara, Via Borsari 46, 44100, Ferrara, Italy.
Biophysical Chemistry
|October 5, 2001
Abstract:
(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. The tensile strength of these filaments changes with the ratio of the fluorescent non-sedimentable actin to the G-actin, being 1.6 pN, 2.9 pN and 3.6 pN at the 1/4, 2/3 and 1/1 ratios, respectively. These tensile strengths are approximately two orders of magnitude lower than those obtained by decoration of F-actin with phalloidin.