dorsal/arxiv
View SchemaWater and molecular chaperones act as weak links of protein folding networks: energy landscape and punctuated equilibrium changes point towards a game theory of proteins
| Authors | Istvan A. Kovacs, Mate S. Szalay, Peter Csermely |
|---|---|
| Categories | |
| ArXiv ID | q-bio/0409030 |
| URL | https://arxiv.org/abs/q-bio/0409030 |
| DOI | 10.1016/j.febslet.2005.03.056 |
| Journal | FEBS Letters (2005) 579: 2254-2260 |
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.
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"abstract": "Water molecules and molecular chaperones efficiently help the protein folding\nprocess. Here we describe their action in the context of the energy and\ntopological networks of proteins. In energy terms water and chaperones were\nsuggested to decrease the activation energy between various local energy minima\nsmoothing the energy landscape, rescuing misfolded proteins from conformational\ntraps and stabilizing their native structure. In kinetic terms water and\nchaperones may make the punctuated equilibrium of conformational changes less\npunctuated and help protein relaxation. Finally, water and chaperones may help\nthe convergence of multiple energy landscapes during protein-macromolecule\ninteractions. We also discuss the possibility of the introduction of protein\ngames to narrow the multitude of the energy landscapes when a protein binds to\nanother macromolecule. Both water and chaperones provide a diffuse set of\nrapidly fluctuating weak links (low affinity and low probability interactions),\nwhich allow the generalization of all these statements to a multitude of\nnetworks.",
"arxiv_id": "q-bio/0409030",
"authors": [
"Istvan A. Kovacs",
"Mate S. Szalay",
"Peter Csermely"
],
"categories": [
"q-bio.BM"
],
"doi": "10.1016/j.febslet.2005.03.056",
"journal_ref": "FEBS Letters (2005) 579: 2254-2260",
"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",
"url": "https://arxiv.org/abs/q-bio/0409030"
},
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