2006/03/01 by Marco Zamparo, Antonio Trovato, Amos Maritan +2
Biochemistry, Genetics and Molecular Biology · Chemistry · Energy · Engineering · Materials Science · Mathematics · Medicine · Physics and Astronomy · #Alzheimer's disease research and treatments #Amyloid fibril #Amyloid β #Chemical engineering #Chemistry #Combinatorics #Compressed hydrogen #Engineering #Enzyme Structure and Function #Folding (DSP implementation) #Fuel Cells and Related Materials #Gravimetric analysis #Hybrid Renewable Energy Systems #Hydrogen #Hydrogen Storage and Materials #Hydrogen fuel #Hydrogen storage #Materials science #Mathematics #Monomer #Nuclear magnetic resonance #Organic chemistry #Phase (matter) #Phase diagram #Physics #Polymer #Protein Structure and Dynamics #Protein folding #Quantum mechanics #Statistical physics #Thermodynamics #cond-mat.stat-mech #q-bio.BM
paper · pdf · doi:10.1103/physrevlett.105.108102
published as Phys. Rev. Lett. 105, 108102 (2010) · 4 pages, 2 figures
openalex publication_date 2006/03/01 · arxiv created 2010/10/21 · arxiv updated 2010/10/22 · openalex created_date 2016/06/24 · openalex updated_date 2026/06/11
We propose an exactly solvable simplified statistical mechanical model for the thermodynamics of β-amyloid aggregation, generalizing a well-studied model for protein folding. The monomer concentration is explicitly taken into account as well as a nontrivial dependence on the microscopic degrees of freedom of the single peptide chain, both in the α-helix folded isolated state and in the fibrillar one. The phase diagram of the model is studied and compared to the outcome of fibril formation experiments which is qualitatively reproduced.