Thermodynamics of aggregation of two proteins

Details Thermodynamics of aggregation of two proteins Thermodynamics of aggregation of two proteins

2006-03-20

arxiv.org/abs/q-bio/0603024v2

Biology

Quantitative Biology

Biomolecules

jpsj2.cls, 7 pages, 14 figures; misconfigurations of Fig.Nos. corrected

Scientific paper

10.1143/JPSJ.75.064803

We investigate aggregation mechanism of two proteins in a thermodynamically unambiguous manner by considering the finite size effect of free energy landscape of HP lattice protein model. Multi-Self-Overlap-Ensemble Monte Carlo method is used for numerical calculations. We find that a dimer can be formed spontaneously as a thermodynamically stable state when the system is small enough. It implies the possibility that the aggregation of proteins in a cell is triggered when they are confined in a small region by, for example, being surrounded by other macromolecules.We also find that the dimer exhibits a transition between unstable state and metastable state in the infinite system.

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