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Part of the book series: IFMBE Proceedings ((IFMBE,volume 49))

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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.

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Correspondence to T. X. Hoang .

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© 2013 IFMBE

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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

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  • 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)

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