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Accurate secondary structure prediction and fold recognition for circular dichroism spectroscopy

Open access
Micsonai, András, Wien, Frank, Kernya, Linda, Lee, Young-Ho, Goto, Yuji, Réfrégiers, Matthieu, Kardos, József·2015·Proceedings of the National Academy of Sciences

Abstract

Significance: Circular dichroism (CD) spectroscopy is widely used for protein secondary structure analysis. However, quantitative estimation for β-sheet–containing proteins is problematic due to the huge morphological and spectral diversity of β-structures. We show that parallel/antiparallel orientation and twisting of β-sheets account for the observed spectral diversity. Taking into account the twist of β-structures, our method accurately estimates the secondary structure for a broad range of protein folds, particularly for β-sheet–rich proteins and amyloid fibrils. Moreover, the method can predict the protein fold down to the topology level following the CATH classification. We provide a general tool for a quick and reliable structure analysis using conventional or synchrotron radiation CD spectroscopy, which is especially useful when X-ray or NMR techniques fail.

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Research works printed but not linked: 38

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Metadata

Authors
Micsonai, A., Wien, F., Kernya, L., Lee, Y.-H., Goto, Y., Réfrégiers, M., & Kardos, J.
Venue
Proceedings of the National Academy of Sciences
Published
2015-06-02
Volume
112
Issue
24
Pages
E3095-103
ISSN
  • 0027-8424 (ISSN-L)
  • 1091-6490
OpenAlex
W1588979652
Cited by
1,703
References
3
FWCI
41.81
Type
journal article
Language
en
Open access
bronze
Funders
  • Országos Tudományos Kutatási Alapprogramok (81950)
  • Hungarian National Research, Development and Innovation Office (KTIA_NAP_13-2-2014-0017)
  • SOLEIL Synchrotron (20140646, 20130475, 20120589, 201110054, 20110405)

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