Simple model study of phase transition properties of isolated and aggregated protein

DOI10.1007/S10955-011-0148-4zbMATH Open1213.82113OpenAlexW2018410486MaRDI QIDQ535052FDOQ535052

Authors: Yong-Yun Ji, Wei-Qi Yi, Lin-Xi Zhang 

Publication date: 11 May 2011

Published in: Journal of Statistical Physics (Search for Journal in Brave)

Full work available at URL: https://doi.org/10.1007/s10955-011-0148-4

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zbMATH Keywords

phase transitionprotein foldingmisfolding diseases

Mathematics Subject Classification ID

Lattice systems (Ising, dimer, Potts, etc.) and systems on graphs arising in equilibrium statistical mechanics (82B20) Phase transitions (general) in equilibrium statistical mechanics (82B26) Statistical mechanics of polymers (82D60)

Cited In (5)

• Schottky-like anomalies and phase transitions in ideal heteropolymer proteinogenic chains in terms of size and single-residue helical propensity
• Cooperative fibril model: native, amyloid-like fibril and unfolded states of proteins
• Thermodiffusion as a close-to-interface effect that matters in non-isothermal (dis)orderly protein aggregations
• Out-of-equilibrium versus dynamical and thermodynamical transitions for a model protein
• On the origin of the phase-space diffusion limit in (dis)ordered protein aggregation

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