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

Ryo Akiyama

doi:10.1007/978-981-10-8459-1_4

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

Ryo Akiyama

Multidisciplinary chemistry

Research output: Chapter in Book/Report/Conference proceeding › Chapter

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.

Original language	English
Title of host publication	The Role of Water in ATP Hydrolysis Energy Transduction by Protein Machinery
Publisher	Springer Singapore
Pages	53-67
Number of pages	15
ISBN (Electronic)	9789811084591
ISBN (Print)	9789811084584
DOIs	https://doi.org/10.1007/978-981-10-8459-1_4
Publication status	Published - May 7 2018

All Science Journal Classification (ASJC) codes

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

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10.1007/978-981-10-8459-1_4

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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 The Role of Water in ATP Hydrolysis Energy Transduction by Protein Machinery (pp. 53-67). Springer Singapore. https://doi.org/10.1007/978-981-10-8459-1_4

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. / Akiyama, Ryo.
The Role of Water in ATP Hydrolysis Energy Transduction by Protein Machinery. Springer Singapore, 2018. p. 53-67.

Research output: Chapter in Book/Report/Conference proceeding › Chapter

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 The Role of Water in ATP Hydrolysis Energy Transduction by Protein Machinery. Springer Singapore, pp. 53-67. https://doi.org/10.1007/978-981-10-8459-1_4

Akiyama R. 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 The Role of Water in ATP Hydrolysis Energy Transduction by Protein Machinery. Springer Singapore. 2018. p. 53-67 doi: 10.1007/978-981-10-8459-1_4

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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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