The role of solvent in protein folding and in aggregation

S. M. Vaiana, M. Manno, A. Emanuele, M. B. Palma-Vittorelli, M. U. Palma

Research output: Contribution to journalArticlepeer-review

30 Scopus citations


We discuss features of the effect of solvent on protein folding and aggregation, highlighting the physics related to the particulate nature and the peculiar structure of the aqueous solvent, and the biological significance of interactions between solvent and proteins. To this purpose we use a generalized energy landscape of extended dimensionality. A closer look at the properties of solvent induced interactions and forces proves useful for understanding the physical grounds of 'ad hoc' interactions and for devising realistic ways of accounting for solvent effects. The solvent has long been known to be a crucially important part of biological systems, and times appear mature for it to be adequately accounted for in the protein folding problem. Use of the extended dimensionality energy landscape helps eliciting the possibility of coupling among conformational changes and aggregation, such as proved by experimental data in the literature.

Original languageEnglish (US)
Pages (from-to)133-145
Number of pages13
JournalJournal of Biological Physics
Issue number2-3
StatePublished - 2001
Externally publishedYes


  • Computational modeling
  • Energy landscapes
  • Hydration
  • Hydrophobic interactions
  • Protein aggregation
  • Protein conformational changes
  • Protein folding
  • Protein-solvent interactions
  • Spinodal and coexistence

ASJC Scopus subject areas

  • Biophysics
  • Atomic and Molecular Physics, and Optics
  • Molecular Biology
  • Cell Biology


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