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Springer Verlag, Ifmbe Proceedings, p. 372-375

DOI: 10.1007/978-3-642-32183-2_90

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Symmetry and Folded Structures of Biomolecules

Proceedings article published in 2013 by T. X. Hoang ORCID, N. T. T. Nhung, J. R. Banavar, A. Maritan
This paper was not found in any repository, but could be made available legally by the author.
This paper was not found in any repository, but could be made available legally by the author.

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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. © 2013 IFMBE.