Determining the role of hydration forces in protein folding

Jon M. Sorenson, Greg Hura, Alan K. Soper, Alexander Pertsemlidis, Teresa Head-Gordon

Research output: Contribution to journalArticlepeer-review

73 Scopus citations

Abstract

This article describes a combined experimental, theoretical, and computational effort to show how the complexity of aqueous hydration can influence the structure, folding and aggregation, and stability of model protein systems. The unification of the theoretical and experimental work is the development or discovery of effective amino acid interactions that implicitly include the effects of aqueous solvent. We show that consideration of the full range of complexity of aqueous hydration forces such as many-body effects, long-ranged character of aqueous solvation, and the assumptions made about the degree of protein hydrophobicity can directly impact the observed structure, folding, and stability of model protein systems.

Original languageEnglish (US)
Pages (from-to)5424-5426
Number of pages3
JournalJournal of Physical Chemistry B
Volume103
Issue number26
DOIs
StatePublished - Jul 1 1999
Externally publishedYes

ASJC Scopus subject areas

  • Physical and Theoretical Chemistry
  • Surfaces, Coatings and Films
  • Materials Chemistry

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