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Thermodynamic Insight into Protein Aggregation Using a Kinetic Ising Model
Author(s) -
Tsai MinYeh,
Yuan JianMin,
Lin ShengHsien
Publication year - 2015
Publication title -
journal of the chinese chemical society
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.329
H-Index - 45
eISSN - 2192-6549
pISSN - 0009-4536
DOI - 10.1002/jccs.201400272
Subject(s) - chemistry , protein aggregation , nucleation , kinetic energy , ising model , work (physics) , fibril , stability (learning theory) , thermodynamics , kinetics , protein stability , statistical physics , chemical physics , physics , biochemistry , organic chemistry , quantum mechanics , machine learning , computer science
In this work, we present a kinetic analysis for protein aggregation using the kinetic Ising model, which serves as a new application of a previously proposed model [Liang et al., J. Chin. Chem. Soc. 2003 , 50 , 335]. Considering protein as a single spin unit, we map two states of a unit to the aggregation‐prone (AP) and the fibril (F) states. This work shows that the model can successfully capture the nucleation‐growth features of protein aggregation from experiments, which offers thermodynamic interpretations of aggregation properties, such as lag‐time and fibril stability.