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Geometry of proteins: Hydrogen bonding, sterics, and marginally compact tubes
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Banavar, Jayanth R., Cieplak, Marek, Flammini, A., Hoang, Trinh X., Kamien, Randall, Lezon, Timothy, Marenduzzo, Davide, Maritan, Amos, Seno, Flavio, Snir, Yehuda and Trovato, Antonio (2006) Geometry of proteins: Hydrogen bonding, sterics, and marginally compact tubes. Physical Review E (Statistical, Nonlinear, and Soft Matter Physics), Vol.73 (No.3 Part 1). Article: 031921. doi:10.1103/PhysRevE.73.031921 ISSN 1539-3755.
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Official URL: http://dx.doi.org/10.1103/PhysRevE.73.031921
Abstract
The functionality of proteins is governed by 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.
Item Type: | Journal Article | ||||
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Subjects: | Q Science > QC Physics | ||||
Divisions: | Faculty of Science, Engineering and Medicine > Science > Mathematics | ||||
Journal or Publication Title: | Physical Review E (Statistical, Nonlinear, and Soft Matter Physics) | ||||
Publisher: | American Physical Society | ||||
ISSN: | 1539-3755 | ||||
Official Date: | March 2006 | ||||
Dates: |
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Volume: | Vol.73 | ||||
Number: | No.3 Part 1 | ||||
Number of Pages: | 5 | ||||
Page Range: | Article: 031921 | ||||
DOI: | 10.1103/PhysRevE.73.031921 | ||||
Status: | Peer Reviewed | ||||
Publication Status: | Published | ||||
Access rights to Published version: | Restricted or Subscription Access | ||||
Funder: | Ministry of Science and Informatics (Poland) (NAUKA), National Science Foundation (U.S.) (NSF) | ||||
Grant number: | 2P03B-032-25 (NAUKA), DGE-9987589 (NSF) |
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