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Journal article
A statistical mechanical approach to protein aggregation
The Journal of chemical physics, v 135(23), pp 235102-235102-12
21 Dec 2011
PMID: 22191902
Featured in Collection : UN Sustainable Development Goals @ Drexel
Abstract
We develop a theory of aggregation using statistical mechanical methods. An example of a complicated aggregation system with several levels of structures is peptide/protein self-assembly. The problem of protein aggregation is important for the understanding and treatment of neurodegenerative diseases and also for the development of bio-macromolecules as new materials. We write the effective Hamiltonian in terms of interaction energies between protein monomers, protein and solvent, as well as between protein filaments. The grand partition function can be expressed in terms of a Zimm-Bragg-like transfer matrix, which is calculated exactly and all thermodynamic properties can be obtained. We start with two-state and three-state descriptions of protein monomers using Potts models that can be generalized to include q-states, for which the exactly solvable feature of the model remains. We focus on n x N lattice systems, corresponding to the ordered structures observed in some real fibrils. We have obtained results on nucleation processes and phase diagrams, in which a protein property such as the sheet content of aggregates is expressed as a function of the number of proteins on the lattice and inter-protein or interfacial interaction energies. We have applied our methods to A beta(1-40) and Curli fibrils and obtained results in good agreement with experiments. (C) 2011 American Institute of Physics. [doi:10.1063/1.3666837]
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Details
- Title
- A statistical mechanical approach to protein aggregation
- Creators
- John S. Schreck - Drexel UniversityJian-Min Yuan - Drexel Univ, Dept Phys, Philadelphia, PA 19104 USA
- Publication Details
- The Journal of chemical physics, v 135(23), pp 235102-235102-12
- Publisher
- American Institute of Physics
- Number of pages
- 12
- Resource Type
- Journal article
- Language
- English
- Academic Unit
- Physics
- Web of Science ID
- WOS:000298539900046
- Scopus ID
- 2-s2.0-84555190701
- Other Identifier
- 991019168652604721
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- Web of Science research areas
- Chemistry, Physical
- Physics, Atomic, Molecular & Chemical