Water and molecular chaperones act as weak links of protein folding networks: Energy landscape and punctuated equilibrium changes point towards a game theory of proteins

István A. Kovács, Máté S. Szalay, Peter Csermely*

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

44 Scopus citations

Abstract

Water molecules and molecular chaperones efficiently help the protein folding process. Here we describe their action in the context of the energy and topological networks of proteins. In energy terms water and chaperones were suggested to decrease the activation energy between various local energy minima smoothing the energy landscape, rescuing misfolded proteins from conformational traps and stabilizing their native structure. In kinetic terms water and chaperones may make the punctuated equilibrium of conformational changes less punctuated and help protein relaxation. Finally, water and chaperones may help the convergence of multiple energy landscapes during protein-macromolecule interactions. We also discuss the possibility of the introduction of protein games to narrow the multitude of the energy landscapes when a protein binds to another macromolecule. Both water and chaperones provide a diffuse set of rapidly fluctuating weak links (low affinity and low probability interactions), which allow the generalization of all these statements to a multitude of networks.

Original languageEnglish (US)
Pages (from-to)2254-2260
Number of pages7
JournalFEBS Letters
Volume579
Issue number11
DOIs
StatePublished - Apr 25 2005

Keywords

  • Chaperone
  • Energy landscape
  • Game theory
  • Protein folding
  • Punctuated equilibrium
  • Water

ASJC Scopus subject areas

  • Biophysics
  • Structural Biology
  • Biochemistry
  • Molecular Biology
  • Genetics
  • Cell Biology

Fingerprint Dive into the research topics of 'Water and molecular chaperones act as weak links of protein folding networks: Energy landscape and punctuated equilibrium changes point towards a game theory of proteins'. Together they form a unique fingerprint.

Cite this