A study of the dynamic properties of actomyosin systems by quasi-elastic light scattering

Amiram Hochberg, William Low, Reuven Tirosh, Julian Borejdo, Avraham Oplatka

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Abstract

A laser light source and a digital autocorrelator were employed in the study of the molecular dynamics of acto-heavy meromyosin during the splitting of ATP. Low protein concentrations were used, so that molecular and not gel properties were evident. The addition of Mg2+ to acto-heavy meromyosin solutions in the presence of ATP caused a marked widening of the spectrum at high scattering angles. No such change was observed when chemically inactivated heavy meromyosin was used, when actin was cross-linked or when the proteins were in a high ionic strength solution. The data can be interpreted in terms of pronounced change in flexibility of acto-heavy meromyosin induced by active mechanochemical coupling.

Original languageEnglish
Pages (from-to)308-317
Number of pages10
JournalBBA - Bioenergetics
Volume460
Issue number2
DOIs
StatePublished - 11 May 1977

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pioglitazone
Myosin Subfragments
Actomyosin
Elastic scattering
Light scattering
Adenosine Triphosphate
Molecular Dynamics Simulation
Ionic strength
Osmolar Concentration
Light sources
Molecular dynamics
Actins
Proteins
Lasers
Gels
Scattering
Light
Dynamic Light Scattering

Cite this

Hochberg, Amiram ; Low, William ; Tirosh, Reuven ; Borejdo, Julian ; Oplatka, Avraham. / A study of the dynamic properties of actomyosin systems by quasi-elastic light scattering. In: BBA - Bioenergetics. 1977 ; Vol. 460, No. 2. pp. 308-317.
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A study of the dynamic properties of actomyosin systems by quasi-elastic light scattering. / Hochberg, Amiram; Low, William; Tirosh, Reuven; Borejdo, Julian; Oplatka, Avraham.

In: BBA - Bioenergetics, Vol. 460, No. 2, 11.05.1977, p. 308-317.

Research output: Contribution to journalArticleResearchpeer-review

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