dorsal/arxiv
View SchemaInternal protein dynamics shifts the distance to the mechanical transition state
| Authors | Daniel K. West, Emanuele Paci, Peter D. Olmsted |
|---|---|
| Categories | |
| ArXiv ID | physics/0612183 |
| URL | https://arxiv.org/abs/physics/0612183 |
| DOI | 10.1103/PhysRevE.74.061912 |
Abstract
Mechanical unfolding of polyproteins by force spectroscopy provides valuable insight into their free energy landscapes. Most phenomenological models of the unfolding process are two-state and/or one dimensional, with the details of the protein and its dynamics often subsumed into a zero-force unfolding rate and a single distance $x_u^{1\textrm{D}}$ to the transition state. We consider the entire phase space of a model protein under a constant force, and show that the distance $x_u^{1\textrm{D}}$ contains a sizeable contribution from exploring the full multidimensional energy landscape. Proteins with more degrees of freedom are expected to have larger values for $x_u^{1\textrm{D}}$. We show that externally attached flexible linkers also contribute to the measured unfolding characteristics.
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"abstract": "Mechanical unfolding of polyproteins by force spectroscopy provides valuable\ninsight into their free energy landscapes. Most phenomenological models of the\nunfolding process are two-state and/or one dimensional, with the details of the\nprotein and its dynamics often subsumed into a zero-force unfolding rate and a\nsingle distance $x_u^{1\\textrm{D}}$ to the transition state. We consider the\nentire phase space of a model protein under a constant force, and show that the\ndistance $x_u^{1\\textrm{D}}$ contains a sizeable contribution from exploring\nthe full multidimensional energy landscape. Proteins with more degrees of\nfreedom are expected to have larger values for $x_u^{1\\textrm{D}}$. We show\nthat externally attached flexible linkers also contribute to the measured\nunfolding characteristics.",
"arxiv_id": "physics/0612183",
"authors": [
"Daniel K. West",
"Emanuele Paci",
"Peter D. Olmsted"
],
"categories": [
"physics.bio-ph"
],
"doi": "10.1103/PhysRevE.74.061912",
"title": "Internal protein dynamics shifts the distance to the mechanical transition state",
"url": "https://arxiv.org/abs/physics/0612183"
},
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