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Accurate secondary structure prediction and fold recognition for circular dichroism spectroscopy
Open accessAbstract
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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Cites
Kabsch, W., & Sander, C. (1983) · Biopolymers · doi:10.1002/bip.360221211 · Cited by 15,320
FTIR reveals structural differences between native β‐sheet proteins and amyloid fibrils
Zandomeneghi, G., Krebs, M. R. H., McCammon, M. G., & Fändrich, M. (2004) · Protein Science · doi:10.1110/ps.041024904 · Cited by 725
Coleman, T. F., & Li, Y. (1996) · SIAM Journal on Optimization · doi:10.1137/s1052623494240456 · Cited by 604
Research works printed but not linked: 38
- 10.1016/0076-6879(95)46006-3 · DOI · Paper page
- 10.1529/biophysj.106.103515 · DOI
- 10.1017/S003358351000003X · DOI
- 10.1107/S0909049500009262 · DOI
- 10.1038/nprot.2006.202 · DOI · Paper page
- B Woollett L Whitmore RW Janes BA Wallace ValiDichro: A website for validating and quality control of protein circular dichroism spectra. Nucleic Acids Res 41(Web Server issue):W417–W421. (2013). · DOI
- 10.1093/nar/gkq1026 · DOI
- 10.1093/bioinformatics/btl327 · DOI · Paper page
- 10.1016/S0022-2836(77)80200-3 · DOI · Paper page
- 10.1016/S0969-2126(97)00260-8 · DOI · Paper page
- 10.1016/j.ab.2009.03.036 · DOI
- 10.1006/abio.2001.5420 · DOI
- 10.1016/j.brainres.2010.07.061 · DOI
- 10.1038/nature02264 · DOI · Paper page
- 10.1110/ps.0235003 · DOI
- 10.1006/jmbi.2001.5385 · DOI
- 10.1016/0022-2836(73)90022-3 · DOI · Paper page
- 10.1016/S0076-6879(73)27030-1 · DOI · Paper page
- 10.1110/ps.8.2.370 · DOI · Paper page
- 10.1021/bi00504a006 · DOI
- 10.1006/abio.2000.4880 · DOI · Paper page
- 10.1186/1471-2105-7-507 · DOI
- 10.1093/protein/5.3.191 · DOI · Paper page
- 10.1016/0003-2697(92)90473-K · DOI
- 10.1016/0003-2697(87)90135-7 · DOI · Paper page
- 10.1016/0003-2697(92)90046-A · DOI · Paper page
- 10.1186/1472-6807-8-25 · DOI · Paper page
- 10.1002/prot.23188 · DOI · Paper page
- 10.1093/bioinformatics/btt278 · DOI · Paper page
- 10.1006/abio.1994.1470 · DOI
- 10.1038/nature05695 · DOI · Paper page
- 10.1016/S0076-6879(04)83013-1 · DOI · Paper page
- 10.1021/jp077462k · DOI
- ATB Gilbert JD Hirst Charge-transfer transitions in protein circular dichroism spectra. Theochem 675(1-3):53–60. (2004). · DOI
- 10.3233/BSI-140098 · DOI
- 10.1039/b200714b · DOI
- 10.1016/S1367-5931(00)00243-X · DOI
- 10.1039/b306055c · DOI
Cited by
Alrosan, M., Tan, T.-C., Easa, A. M., Gammoh, S., & Alu'datt, M. H. (2022) · Critical Reviews in Food Science and Nutrition · doi:10.1080/10408398.2021.1871589 · Cited by 104
McAvan, B. S., Bowsher, L. A., Powell, T., O’Hara, J. F., Spitali, M., Goodacre, R., & Doig, A. J. (2020) · Analytical Chemistry · doi:10.1021/acs.analchem.0c00627 · Cited by 61
Origin of the Reflectin Gene and Hierarchical Assembly of Its Protein
Guan, Z., Cai, T., Liu, Z., Dou, Y., Hu, X., Zhang, P., Sun, X., Li, H., Kuang, Y., Zhai, Q., et al. (2017) · Current Biology · doi:10.1016/j.cub.2017.07.061 · Cited by 52
Sharma, S., Nehru, B., & Saini, A. (2017) · Neurochemistry International · doi:10.1016/j.neuint.2017.06.011 · Cited by 48
MOSPD2 is an endoplasmic reticulum–lipid droplet tether functioning in LD homeostasis
Zouiouich, M., Di Mattia, T., Martinet, A., Eichler, J., Wendling, C., Tomishige, N., Grandgirard, E., Fuggetta, N., Fromental-Ramain, C., Mizzon, G., et al. (2022) · Journal of Cell Biology · doi:10.1083/jcb.202110044 · Cited by 40
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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- Micsonai, A., Wien, F., Kernya, L., Lee, Y.-H., Goto, Y., Réfrégiers, M., & Kardos, J. (2015). Accurate secondary structure prediction and fold recognition for circular dichroism spectroscopy. Proceedings of the National Academy of Sciences. https://doi.org/10.1073/pnas.1500851112
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