(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.

On the elastic properties of tetramethylrhodamine F-actin / O. Cintio, R. Adami, D. Choquet, E. Grazi. - In: BIOPHYSICAL CHEMISTRY. - ISSN 0301-4622. - 92:3(2001 Sep 18), pp. 201-207.

On the elastic properties of tetramethylrhodamine F-actin

R. Adami
Secondo
;
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.
F-actin; Phalloidin; Rhodamine; Tensile strength
Settore BIO/09 - Fisiologia
Settore BIO/10 - Biochimica
Settore BIO/11 - Biologia Molecolare
Settore BIO/13 - Biologia Applicata
Settore BIO/06 - Anatomia Comparata e Citologia
Settore BIO/17 - Istologia
18-set-2001
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Utilizza questo identificativo per citare o creare un link a questo documento: https://hdl.handle.net/2434/209349
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