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

Research output: Chapter in Book/Report/Conference proceedingChapter

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 languageEnglish
Title of host publicationThe Role of Water in ATP Hydrolysis Energy Transduction by Protein Machinery
PublisherSpringer Singapore
Pages53-67
Number of pages15
ISBN (Electronic)9789811084591
ISBN (Print)9789811084584
DOIs
Publication statusPublished - May 7 2018

All Science Journal Classification (ASJC) codes

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

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