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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(s) -
Kovács István A.,
Szalay Máté S.,
Csermely Peter
Publication year - 2005
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2005.03.056
Subject(s) - energy landscape , protein folding , folding (dsp implementation) , context (archaeology) , folding funnel , protein structure , biophysics , chemistry , chemical physics , biology , downhill folding , biochemistry , phi value analysis , electrical engineering , engineering , paleontology
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.