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National Academy of Sciences, Proceedings of the National Academy of Sciences, 22(95), p. 12930-12933, 1998

DOI: 10.1073/pnas.95.22.12930

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Folding and aggregation of designed proteins

Journal article published in 1998 by R. A. Broglia, G. Tiana ORCID, S. Pasquali, H. E. Roman, E. Vigezzi
This paper is made freely available by the publisher.
This paper is made freely available by the publisher.

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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.