Novel intermolecular surface force unveils the driving force of the actomyosin system

Makoto Suzuki, George Mogami, Takahiro Watanabe, Nobuyuki Matubayasi

Research output: Chapter in Book/Report/Conference proceedingChapter

Abstract

In this chapter, we discuss the role of water in actomyosin-force generation. We have been investigating the hydration properties of ions, organic molecules, and proteins. These studies revealed that actin filaments (F-actin) are surrounded by a hyper-mobile water (HMW) layer and restrained water layer, while myosin subfragment 1 (S1) has only a typical restrained hydration layer. The understanding of the physicochemical properties of HMW has been greatly advanced by recent theoretical studies on statistical mechanics and solution chemistry. To explain the mechanism of force generation of actomyosin using ATP hydrolysis, we propose a driving force hypothesis based on novel intermolecular surface force. This hypothesis is consistent with the reported biochemical kinetics and thermodynamic parameters for the primary reaction steps. The gradient field of solvation free energy of S1 is generated in close proximity to F-actin.

Original languageEnglish
Title of host publicationThe Role of Water in ATP Hydrolysis Energy Transduction by Protein Machinery
PublisherSpringer Singapore
Pages257-274
Number of pages18
ISBN (Electronic)9789811084591
ISBN (Print)9789811084584
DOIs
Publication statusPublished - 2018 May 7

Keywords

  • ATP hydrolysis
  • Electric field effect
  • Hydration free energy motor protein
  • Protein-water interaction

ASJC Scopus subject areas

  • Chemistry(all)
  • Biochemistry, Genetics and Molecular Biology(all)

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    Suzuki, M., Mogami, G., Watanabe, T., & Matubayasi, N. (2018). Novel intermolecular surface force unveils the driving force of the actomyosin system. In The Role of Water in ATP Hydrolysis Energy Transduction by Protein Machinery (pp. 257-274). Springer Singapore. https://doi.org/10.1007/978-981-10-8459-1_16