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

  title={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},
  author={Istv{\'a}n A. Kov{\'a}cs and Mate S. Szalay and P. Csermely},
  journal={FEBS Letters},
  • István A. Kovács, Mate S. Szalay, P. Csermely
  • Published 2005
  • Medicine, Biology
  • FEBS Letters
  • 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… CONTINUE READING
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    • 184
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    • 252
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    • 2,108
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    • Cellular and molecular biology
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    • 20
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    • 75
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    • K. Dill
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    • Protein science : a publication of the Protein Society
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