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

0Citations
Citations of this article
1Readers
Mendeley users who have this article in their library.
Get full text

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.

Cite

CITATION STYLE

APA

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

Register to see more suggestions

Mendeley helps you to discover research relevant for your work.

Already have an account?

Save time finding and organizing research with Mendeley

Sign up for free