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.
|Title of host publication||The Role of Water in ATP Hydrolysis Energy Transduction by Protein Machinery|
|Number of pages||15|
|Publication status||Published - May 7 2018|
All Science Journal Classification (ASJC) codes
- Biochemistry, Genetics and Molecular Biology(all)