Interaction of myosin subfragment 1 with F-actin studied by differential scanning calorimetry

Olga P. Nikolaeva; Victor N. Orlov; Irina V. Dedova; Vladimir A. Drachev; Dmitrii I. Levitsky

doi:10.1080/15216549600201253

Interaction of myosin subfragment 1 with F-actin studied by differential scanning calorimetry

Olga P. Nikolaeva, Victor N. Orlov, Irina V. Dedova, Vladimir A. Drachev, Dmitrii I. Levitsky^*

^*Corresponding author for this work

Research output: Contribution to journal › Article › peer-review

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Abstract

The thermal unfolding of the myosin subfragment 1 (S1) and of filamentous actin (F-actin) in their strong complex obtained in the presence of ADP was studied by differential scanning calorimetry (DSC). It is shown that in the acto-S1 complexes S1 and F-actin melt separately, and thermal transitions of each protein can be easily followed. Interaction of S1 with F-actin significantly increases S1 thermal stability and also affects the thermal stability of F-actin. Although S1 unfolds at much lower temperature than F-actin, the molecules of S1 remain bound to F-actin even after full denaturation. Under these conditions S1 may induce cross-linking between actin filaments. It is concluded that DSC studies on the acto-S1 complexes offer a new and promising approach to investigate the structural changes which occur in the myosin head and in F-actin due to their interaction.

Original language	English
Pages (from-to)	653-661
Number of pages	9
Journal	Biochemistry and Molecular Biology International
Volume	40
Issue number	4
DOIs	https://doi.org/10.1080/15216549600201253
Publication status	Published - Nov 1996
Externally published	Yes

Keywords

Differential scanning calorimetry
F-actin
Myosin subfragment 1

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10.1080/15216549600201253

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title = "Interaction of myosin subfragment 1 with F-actin studied by differential scanning calorimetry",

abstract = "The thermal unfolding of the myosin subfragment 1 (S1) and of filamentous actin (F-actin) in their strong complex obtained in the presence of ADP was studied by differential scanning calorimetry (DSC). It is shown that in the acto-S1 complexes S1 and F-actin melt separately, and thermal transitions of each protein can be easily followed. Interaction of S1 with F-actin significantly increases S1 thermal stability and also affects the thermal stability of F-actin. Although S1 unfolds at much lower temperature than F-actin, the molecules of S1 remain bound to F-actin even after full denaturation. Under these conditions S1 may induce cross-linking between actin filaments. It is concluded that DSC studies on the acto-S1 complexes offer a new and promising approach to investigate the structural changes which occur in the myosin head and in F-actin due to their interaction.",

keywords = "Differential scanning calorimetry, F-actin, Myosin subfragment 1",

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T1 - Interaction of myosin subfragment 1 with F-actin studied by differential scanning calorimetry

AU - Nikolaeva, Olga P.

AU - Orlov, Victor N.

AU - Dedova, Irina V.

AU - Drachev, Vladimir A.

AU - Levitsky, Dmitrii I.

PY - 1996/11

Y1 - 1996/11

N2 - The thermal unfolding of the myosin subfragment 1 (S1) and of filamentous actin (F-actin) in their strong complex obtained in the presence of ADP was studied by differential scanning calorimetry (DSC). It is shown that in the acto-S1 complexes S1 and F-actin melt separately, and thermal transitions of each protein can be easily followed. Interaction of S1 with F-actin significantly increases S1 thermal stability and also affects the thermal stability of F-actin. Although S1 unfolds at much lower temperature than F-actin, the molecules of S1 remain bound to F-actin even after full denaturation. Under these conditions S1 may induce cross-linking between actin filaments. It is concluded that DSC studies on the acto-S1 complexes offer a new and promising approach to investigate the structural changes which occur in the myosin head and in F-actin due to their interaction.

AB - The thermal unfolding of the myosin subfragment 1 (S1) and of filamentous actin (F-actin) in their strong complex obtained in the presence of ADP was studied by differential scanning calorimetry (DSC). It is shown that in the acto-S1 complexes S1 and F-actin melt separately, and thermal transitions of each protein can be easily followed. Interaction of S1 with F-actin significantly increases S1 thermal stability and also affects the thermal stability of F-actin. Although S1 unfolds at much lower temperature than F-actin, the molecules of S1 remain bound to F-actin even after full denaturation. Under these conditions S1 may induce cross-linking between actin filaments. It is concluded that DSC studies on the acto-S1 complexes offer a new and promising approach to investigate the structural changes which occur in the myosin head and in F-actin due to their interaction.

KW - Differential scanning calorimetry

KW - F-actin

KW - Myosin subfragment 1

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Interaction of myosin subfragment 1 with F-actin studied by differential scanning calorimetry

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Keywords

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