dorsal/arxiv
View SchemaCooperativity and Contact Order in Protein Folding
| Authors | Marek Cieplak |
|---|---|
| Categories | |
| ArXiv ID | q-bio/0401017 |
| URL | https://arxiv.org/abs/q-bio/0401017 |
| DOI | 10.1103/PhysRevE.69.031907 |
Abstract
The effects of cooperativity are studied within Go-Lennard-Jones models of proteins by making the contact interactions dependent on the proximity to the native conformation. The kinetic universality classes are found to remain the same as in the absence of cooperativity. For a fixed native geometry, small changes in the effective contact map may affect the folding times in a chance way and to the extent that is comparable to the shift in the folding times due to cooperativity. The contact order controlls folding scenarios: the average times necessary to bring pairs of amino acids into their near native separations depend on the sequential distances within the pairs. This dependence is largely monotonic, regardless of the cooperativity, and the dominant trend could be described by a single parameter like the average contact order. However, it is the deviations from the trend which are usually found to set the net folding times.
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"abstract": "The effects of cooperativity are studied within Go-Lennard-Jones models of\nproteins by making the contact interactions dependent on the proximity to the\nnative conformation. The kinetic universality classes are found to remain the\nsame as in the absence of cooperativity. For a fixed native geometry, small\nchanges in the effective contact map may affect the folding times in a chance\nway and to the extent that is comparable to the shift in the folding times due\nto cooperativity. The contact order controlls folding scenarios: the average\ntimes necessary to bring pairs of amino acids into their near native\nseparations depend on the sequential distances within the pairs. This\ndependence is largely monotonic, regardless of the cooperativity, and the\ndominant trend could be described by a single parameter like the average\ncontact order. However, it is the deviations from the trend which are usually\nfound to set the net folding times.",
"arxiv_id": "q-bio/0401017",
"authors": [
"Marek Cieplak"
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"q-bio.BM",
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"doi": "10.1103/PhysRevE.69.031907",
"title": "Cooperativity and Contact Order in Protein Folding",
"url": "https://arxiv.org/abs/q-bio/0401017"
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