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Thermodynamic and Evolutionary Coupling between the Native and Amyloid State of Globular Proteins

Authors
  • Langenberg, Tobias1, 2
  • Gallardo, Rodrigo1, 2
  • van der Kant, Rob1, 2
  • Louros, Nikolaos1, 2
  • Michiels, Emiel1, 2
  • Duran-Romaña, Ramon1, 2
  • Houben, Bert1, 2
  • Cassio, Rafaela1, 2
  • Wilkinson, Hannah1, 2
  • Garcia, Teresa1, 2
  • Ulens, Chris3
  • Van Durme, Joost1, 2
  • Rousseau, Frederic1, 2
  • Schymkowitz, Joost1, 2
  • 1 Switch Laboratory, VIB Center for Brain and Disease Research, Herestraat 49, 3000 Leuven, Belgium
  • 2 Switch Laboratory, Department of Cellular and Molecular Medicine, KU Leuven, Herestraat 49, 3000 Leuven, Belgium
  • 3 Laboratory of Structural Neurobiology, Department of Cellular and Molecular Medicine, KU Leuven, Herestraat 49, 3000 Leuven, Belgium
Type
Published Article
Journal
Cell Reports
Publisher
Elsevier
Publication Date
Apr 14, 2020
Volume
31
Issue
2
Identifiers
DOI: 10.1016/j.celrep.2020.03.076
PMID: 32294448
PMCID: PMC7175379
Source
PubMed Central
Keywords
License
Unknown

Abstract

Langenberg et al. show that amyloid propensity favors protein stability. This results from the energetic correlation of mutation in the native and amyloid state. The genetic code tightens this relationship so that stable amyloidogenic sequences are deeply conserved. Positive selection of amyloidogenic sequences could therefore have favored the evolution of globular structure.

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