dorsal/arxiv
View SchemaStretching of Proteins in the Entropic Limit
| Authors | Marek Cieplak, Trinh Xuan Hoang, Mark O. Robbins |
|---|---|
| Categories | |
| ArXiv ID | q-bio/0311015 |
| URL | https://arxiv.org/abs/q-bio/0311015 |
| DOI | 10.1103/PhysRevE.69.011912 |
Abstract
Mechanical stretching of six proteins is studied through molecular dynamics simulations. The model is Go-like, with Lennard-Jones interactions at native contacts. Low temperature unfolding scenarios are remarkably complex and sensitive to small structural changes. Thermal fluctuations reduce the peak forces and the number of metastable states during unfolding. The unfolding pathways also simplify as temperature rises. In the entropic limit, all proteins show a monotonic decrease of the extension where bonds rupture with their separation along the backbone (contact order).
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"abstract": "Mechanical stretching of six proteins is studied through molecular dynamics\nsimulations. The model is Go-like, with Lennard-Jones interactions at native\ncontacts. Low temperature unfolding scenarios are remarkably complex and\nsensitive to small structural changes. Thermal fluctuations reduce the peak\nforces and the number of metastable states during unfolding. The unfolding\npathways also simplify as temperature rises. In the entropic limit, all\nproteins show a monotonic decrease of the extension where bonds rupture with\ntheir separation along the backbone (contact order).",
"arxiv_id": "q-bio/0311015",
"authors": [
"Marek Cieplak",
"Trinh Xuan Hoang",
"Mark O. Robbins"
],
"categories": [
"q-bio.BM",
"cond-mat.soft",
"q-bio.QM"
],
"doi": "10.1103/PhysRevE.69.011912",
"title": "Stretching of Proteins in the Entropic Limit",
"url": "https://arxiv.org/abs/q-bio/0311015"
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