dorsal/arxiv
View SchemaMechanical properties of the domains of titin in a Go-like model
| Authors | Marek Cieplak, Annalisa Pastore, Trinh Xuan Hoang |
|---|---|
| Categories | |
| ArXiv ID | q-bio/0411022 |
| URL | https://arxiv.org/abs/q-bio/0411022 |
| DOI | 10.1063/1.1839572 |
Abstract
Comparison of properties of three domains of titin, I1, I27 and I28, in a simple geometry-based model shows that despite a high structural homology between their native states different domains show similar but distinguishable mechanical properties. Folding properties of the separate domains are predicted to be diversified which reflects sensitivity of the kinetics to the details of native structures. The Go-like model corresponding to the experimentally resolved native structure of the I1 domain is found to provide the biggest thermodynamic and mechanical stability compared to the other domains studied here. We analyze elastic, thermodynamic and kinetic properties of several structures corresponding to the I28 domain as obtained through homology-based modeling. We discuss the ability of the models of the I28 domain to reproduce experimental results qualitatively. A strengthening of contacts that involve hydrophobic amino acids does not affect theoretical comparisons of the domains. Tandem linkages of up to five identical or different domains unravel in a serial fashion at low temperatures. We study the nature of the intermediate state that arises in the early stages of the serial unraveling and find it to qualitatively agree with the results of Marszalek et al.
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"abstract": "Comparison of properties of three domains of titin, I1, I27 and I28, in a\nsimple geometry-based model shows that despite a high structural homology\nbetween their native states different domains show similar but distinguishable\nmechanical properties. Folding properties of the separate domains are predicted\nto be diversified which reflects sensitivity of the kinetics to the details of\nnative structures. The Go-like model corresponding to the experimentally\nresolved native structure of the I1 domain is found to provide the biggest\nthermodynamic and mechanical stability compared to the other domains studied\nhere. We analyze elastic, thermodynamic and kinetic properties of several\nstructures corresponding to the I28 domain as obtained through homology-based\nmodeling. We discuss the ability of the models of the I28 domain to reproduce\nexperimental results qualitatively. A strengthening of contacts that involve\nhydrophobic amino acids does not affect theoretical comparisons of the domains.\nTandem linkages of up to five identical or different domains unravel in a\nserial fashion at low temperatures. We study the nature of the intermediate\nstate that arises in the early stages of the serial unraveling and find it to\nqualitatively agree with the results of Marszalek et al.",
"arxiv_id": "q-bio/0411022",
"authors": [
"Marek Cieplak",
"Annalisa Pastore",
"Trinh Xuan Hoang"
],
"categories": [
"q-bio.BM",
"cond-mat.soft"
],
"doi": "10.1063/1.1839572",
"title": "Mechanical properties of the domains of titin in a Go-like model",
"url": "https://arxiv.org/abs/q-bio/0411022"
},
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