TY - CHAP
T1 - Theoretical studies of strong attractive interaction between macro-anions mediated by multivalent metal cations and related association behavior
T2 - Effective interaction between ATP-binding proteins can be regulated by hydrolysis
AU - Akiyama, Ryo
PY - 2018/5/7
Y1 - 2018/5/7
N2 - 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.
AB - 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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U2 - 10.1007/978-981-10-8459-1_4
DO - 10.1007/978-981-10-8459-1_4
M3 - Chapter
AN - SCOPUS:85053985142
SN - 9789811084584
SP - 53
EP - 67
BT - The Role of Water in ATP Hydrolysis Energy Transduction by Protein Machinery
PB - Springer Singapore
ER -