Abstract
Our work suggests that protein native state structures occupy a novel phase of matter corresponding to the marginally compact conformations of a flexible tube. This phase arises from common attributes of proteins and is independent of amino acid sequences. Our approach provides a simple and unified framework to understand protein folding and amyloid formation. With a constraint on the local radius of curvature, the tube model is also shown to have ground state conformations similar to that of DNA toroids.
Access this chapter
Tax calculation will be finalised at checkout
Purchases are for personal use only
Preview
Unable to display preview. Download preview PDF.
Author information
Authors and Affiliations
Corresponding author
Editor information
Editors and Affiliations
Rights and permissions
Copyright information
© 2013 IFMBE
About this paper
Cite this paper
Hoang, T.X., Nhung, N.T.T., Banavar, J.R., Maritan, A. (2013). Symmetry and Folded Structures of Biomolecules. In: Toi, V., Toan, N., Dang Khoa, T., Lien Phuong, T. (eds) 4th International Conference on Biomedical Engineering in Vietnam. IFMBE Proceedings, vol 49. Springer, Berlin, Heidelberg. https://doi.org/10.1007/978-3-642-32183-2_90
Download citation
DOI: https://doi.org/10.1007/978-3-642-32183-2_90
Publisher Name: Springer, Berlin, Heidelberg
Print ISBN: 978-3-642-32182-5
Online ISBN: 978-3-642-32183-2
eBook Packages: EngineeringEngineering (R0)