Abstract

This work reviews both the theory and experimental measurements of the fundamental forces that control protein solution behavior. In addition to the Derjaguin-Landau-Verwey-Overbeek (DLVO) forces, we also discuss the relative importance of hydrodynamic, solvation, and lock-and-key interactions in controlling protein solution behavior. The more common computational methods used to calculate both electrostatic and van der Waals potentials are described. Particular attention is given to the differences between proteins and ideal colloidal particles, and the computational methods used to address those differences. In addition to theoretical investigations of protein interactions, the results of recent direct measurements of the forces governing protein interactions are reviewed. These experimental results provide not only measurements against which the theories can be tested, but also demonstrate directly the relative importance of both DLVO and non-classical DLVO forces in the control of protein behavior. Copyright (C) 1999 Elsevier Science B.V.

Original languageEnglish (US)
Pages (from-to)83-97
Number of pages15
JournalColloids and Surfaces B: Biointerfaces
Volume14
Issue number1-4
DOIs
StatePublished - Aug 1999

Keywords

  • DLVO forces
  • Protein solution behavior
  • Van der Waals forces

ASJC Scopus subject areas

  • Biotechnology
  • Colloid and Surface Chemistry
  • Physical and Theoretical Chemistry
  • Surfaces and Interfaces

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