dorsal/arxiv
View SchemaGeometry of proteins: hydrogen bonding, sterics and marginally compact tubes
| Authors | Jayanth R. Banavar, Marek Cieplak, Alessandro Flammini, Trinh X. Hoang, Randall D. Kamien, Timothy Lezon, Davide Marenduzzo, Amos Maritan, Flavio Seno, Yehuda Snir, Antonio Trovato |
|---|---|
| Categories | |
| ArXiv ID | q-bio/0505052 |
| URL | https://arxiv.org/abs/q-bio/0505052 |
| DOI | 10.1103/PhysRevE.73.031921 |
Abstract
The functionality of proteins is related to their structure in the native state. Protein structures are made up of emergent building blocks of helices and almost planar sheets. A simple coarse-grained geometrical model of a flexible tube barely subject to compaction provides a unified framework for understanding the common character of globular proteins.We argue that a recent critique of the tube idea is not well founded.
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"abstract": "The functionality of proteins is related to their structure in the native\nstate. Protein structures are made up of emergent building blocks of helices\nand almost planar sheets. A simple coarse-grained geometrical model of a\nflexible tube barely subject to compaction provides a unified framework for\nunderstanding the common character of globular proteins.We argue that a recent\ncritique of the tube idea is not well founded.",
"arxiv_id": "q-bio/0505052",
"authors": [
"Jayanth R. Banavar",
"Marek Cieplak",
"Alessandro Flammini",
"Trinh X. Hoang",
"Randall D. Kamien",
"Timothy Lezon",
"Davide Marenduzzo",
"Amos Maritan",
"Flavio Seno",
"Yehuda Snir",
"Antonio Trovato"
],
"categories": [
"q-bio.BM"
],
"doi": "10.1103/PhysRevE.73.031921",
"title": "Geometry of proteins: hydrogen bonding, sterics and marginally compact tubes",
"url": "https://arxiv.org/abs/q-bio/0505052"
},
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"source": {
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