期刊
PHYSICAL REVIEW LETTERS
卷 105, 期 10, 页码 -出版社
AMER PHYSICAL SOC
DOI: 10.1103/PhysRevLett.105.108102
关键词
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资金
- Italian Ministry of Education, University and Research [PRIN 2007B57EAB]
- University of Padua via Progetto di Ateneo [CPDA083702]
We propose an exactly solvable simplified statistical mechanical model for the thermodynamics of beta-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 alpha-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.
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