| Literature DB >> 9789017 |
R A Broglia1, G Tiana, S Pasquali, H E Roman, E Vigezzi.
Abstract
Protein aggregation is studied by following the simultaneous folding of two designed identical 20-letter amino acid chains within the framework of a lattice model and using Monte Carlo simulations. It is found that protein aggregation is determined by elementary structures (partially folded intermediates) controlled by local contacts among some of the most strongly interacting amino acids and formed at an early stage in the folding process.Entities:
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Year: 1998 PMID: 9789017 PMCID: PMC23658 DOI: 10.1073/pnas.95.22.12930
Source DB: PubMed Journal: Proc Natl Acad Sci U S A ISSN: 0027-8424 Impact factor: 11.205