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Theoretical Studies of Strong Attractive Interaction Between Macro-anions Mediated by Multivalent Metal Cations and Related Association Behavior: Effective Interaction Between ATP-Binding Proteins Can Be Regulated by Hydrolysis

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The Role of Water in ATP Hydrolysis Energy Transduction by Protein Machinery

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Abstract

In this chapter, calculated effective interactions between macro-anions are introduced. The macro-anions are effectively attracted to each other under certain conditions, and the aggregation behavior of macro-anions is discussed on the basis of the calculated effective interactions. The success of models that simulate the behavior of such systems indicates that theoretical discussions are important to understanding the observed aggregation of acidic proteins in solution of multivalent cations. The hydrolysis of ATP regulates the effective interaction between ATP-binding proteins, such as actin monomers. The regulation of effective interaction is discussed from the viewpoint of the calculated effective interaction between macro-anions.

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Authors and Affiliations

  1. Department of Chemistry, Kyushu University, Fukuoka, Japan

    Ryo Akiyama

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  1. Ryo Akiyama
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Correspondence to Ryo Akiyama .

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Editors and Affiliations

  1. Institute of Engineering Education, Tohoku University, Sendai, Miyagi, Japan

    Makoto Suzuki

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Akiyama, R. (2018). Theoretical Studies of Strong Attractive Interaction Between Macro-anions Mediated by Multivalent Metal Cations and Related Association Behavior: Effective Interaction Between ATP-Binding Proteins Can Be Regulated by Hydrolysis. In: Suzuki, M. (eds) The Role of Water in ATP Hydrolysis Energy Transduction by Protein Machinery. Springer, Singapore. https://doi.org/10.1007/978-981-10-8459-1_4

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