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Compactness, aggregation, and prionlike behavior of protein: A lattice model study

G. GIUGLIARELLI
•
J. R. BANAVAR
•
A. MARITAN
•
Micheletti, Cristian
2000
  • journal article

Periodico
THE JOURNAL OF CHEMICAL PHYSICS
Abstract
The solubility and compactness of proteins is investigated within the framework of models amenable to an exact numerical study through exhaustive enumeration. We study how the average inter-amino acid interaction potential affects the properties of both isolated and interacting proteins. In a concentrated solution, depending on the value of the average potential, individual proteins may remain stable in the isolated native structure (soluble case), may aggregate preserving their geometrical shape (nonsoluble case) or aggregate changing their geometrical shape (prionlike behavior). The number of sequences that have compact native states and are soluble is maximal at a fine-tuned average interaction potential and of the same order of the corresponding number of nonsoluble prionlike proteins. The viable protein sequences selected by such a fine-tuned potential are found to have an amino acid composition similar to naturally occurring proteins.
DOI
10.1063/1.1289463
WOS
WOS:000089173200028
Archivio
http://hdl.handle.net/20.500.11767/16530
info:eu-repo/semantics/altIdentifier/scopus/2-s2.0-0034275017
Diritti
closed access
Scopus© citazioni
44
Data di acquisizione
Jun 14, 2022
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Web of Science© citazioni
42
Data di acquisizione
Mar 28, 2024
Visualizzazioni
2
Data di acquisizione
Apr 19, 2024
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