The DOI matches its Crossref record; 32 of the 32 references it cites were found in a registry or an index.
DichroWeb, a website for calculating protein secondary structure from circular dichroism spectroscopic data
Open accessAbstract
Circular dichroism (CD) spectroscopy is a widely‐used method for characterizing the secondary structures of proteins. The well‐established and highly used analysis website, DichroWeb (located at: http://dichroweb.cryst.bbk.ac.uk/html/home.shtml) enables the facile quantitative determination of helix, sheet, and other secondary structure contents of proteins based on their CD spectra. DichroWeb includes a range of reference datasets and algorithms, plus graphical and quantitative methods for determining the quality of the analyses produced. This article describes the current website content, usage and accessibility, as well as the many upgraded features now present in this highly popular tool that was originally created nearly two decades ago.
Overview
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Citations
Cites
Kabsch, W., & Sander, C. (1983) · Biopolymers · doi:10.1002/bip.360221211 · Cited by 15,320
Using circular dichroism spectra to estimate protein secondary structure
Greenfield, N. J. (2006) · Nature Protocols · doi:10.1038/nprot.2006.202 · Cited by 4,014
Sreerama, N., & Woody, R. W. (2000) · Analytical Biochemistry · doi:10.1006/abio.2000.4880 · Cited by 2,992
Whitmore, L., & Wallace, B. A. (2004) · Nucleic Acids Research · doi:10.1093/nar/gkh371 · Cited by 2,338
Self-citationWhitmore, L., & Wallace, B. A. (2008) · Biopolymers · doi:10.1002/bip.20853 · Cited by 2,243
Self-citationEstimation of globular protein secondary structure from circular dichroism
Provencher, S. W., & Gloeckner, J. (1981) · Biochemistry · doi:10.1021/bi00504a006 · Cited by 2,155
Circular Dichroism and the Conformational Analysis of Biomolecules
(1996) · Springer eBooks · doi:10.1007/978-1-4757-2508-7 · Cited by 1,930
Micsonai, A., Wien, F., Bulyáki, É., Kun, J., Moussong, É., Lee, Y.-H., Goto, Y., Réfrégiers, M., & Kardos, J. (2018) · Nucleic Acids Research · doi:10.1093/nar/gky497 · Cited by 1,131
The worldwide Protein Data Bank (wwPDB): ensuring a single, uniform archive of PDB data
Berman, H., Henrick, K., Nakamura, H., & Markley, J. L. (2007) · Nucleic Acids Research · doi:10.1093/nar/gkl971 · Cited by 1,125
A Self-Consistent Method for the Analysis of Protein Secondary Structure from Circular Dichroism
Sreerama, N., & Woody, R. W. (1993) · Analytical Biochemistry · doi:10.1006/abio.1993.1079 · Cited by 1,045
Andrade, M. A., Chacón, P., Merelo, J. J., & Morán, F. (1993) · "Protein Engineering, Design and Selection" · doi:10.1093/protein/6.4.383 · Cited by 1,007
Louis‐Jeune, C., Andrade‐Navarro, M. A., & Perez‐Iratxeta, C. (2012) · Proteins: Structure, Function, and Bioinformatics · doi:10.1002/prot.23188 · Cited by 742
Lobley, A., Whitmore, L., & Wallace, B. A. (2002) · Bioinformatics · doi:10.1093/bioinformatics/18.1.211 · Cited by 726
Self-citationSreerama, N., Venyaminov, S. Y. U., & Woody, R. W. (1999) · Protein Science · doi:10.1110/ps.8.2.370 · Cited by 708
Manavalan, P., & Johnson, W. C. (1987) · Analytical Biochemistry · doi:10.1016/0003-2697(87)90135-7 · Cited by 706
Sreerama, N., Venyaminov, S. Y., & Woody, R. W. (2000) · Analytical Biochemistry · doi:10.1006/abio.2000.4879 · Cited by 582
Compton, L. A., & Johnson, W. C. (1986) · Analytical Biochemistry · doi:10.1016/0003-2697(86)90241-1 · Cited by 569
Estimation of protein secondary structure and error analysis from circular dichroism spectra
van Stokkum, I. H. M., Spoelder, H. J. W., Bloemendal, M., van Grondelle, R., & Groen, F. C. A. (1990) · Analytical Biochemistry · doi:10.1016/0003-2697(90)90396-q · Cited by 502
K2D2: Estimation of protein secondary structure from circular dichroism spectra
Perez-Iratxeta, C., & Andrade-Navarro, M. A. (2008) · BMC Structural Biology · doi:10.1186/1472-6807-8-25 · Cited by 470
Perczel, A., Park, K., & Fasman, G. D. (1992) · Analytical Biochemistry · doi:10.1016/0003-2697(92)90046-a · Cited by 430
A reference database for circular dichroism spectroscopy covering fold and secondary structure space
Lees, J. G., Miles, A. J., Wien, F., & Wallace, B. A. (2006) · Bioinformatics · doi:10.1093/bioinformatics/btl327 · Cited by 423
Self-citationCircular dichroism spectroscopy of membrane proteins
Miles, A. J., & Wallace, B. A. (2016) · Chemical Society Reviews · doi:10.1039/c5cs00084j · Cited by 368
Self-citationTools and methods for circular dichroism spectroscopy of proteins: a tutorial review
Miles, A. J., Janes, R. W., & Wallace, B. A. (2021) · Chemical Society Reviews · doi:10.1039/d0cs00558d · Cited by 345
Self-citationLees, J. G., Smith, B. R., Wien, F., Miles, A. J., & Wallace, B. A. (2004) · Analytical Biochemistry · doi:10.1016/j.ab.2004.06.002 · Cited by 263
Self-citationMiles, A. J., & Wallace, B. A. (2006) · Chem. Soc. Rev. · doi:10.1039/b316168b · Cited by 241
Self-citationLopes, J. L. S., Miles, A. J., Whitmore, L., & Wallace, B. A. (2014) · Protein Science · doi:10.1002/pro.2558 · Cited by 216
Self-citationMao, D., Wachter, E., & Wallace, B. A. (1982) · Biochemistry · doi:10.1021/bi00263a020 · Cited by 183
Self-citationAbdul-Gader, A., Miles, A. J., & Wallace, B. A. (2011) · Bioinformatics · doi:10.1093/bioinformatics/btr234 · Cited by 168
Self-citationMiles, A. J., & Wallace, B. A. (2018) · Protein Science · doi:10.1002/pro.3474 · Cited by 150
Self-citationWallace, B. A., & Janes, R. W. (2009) · BIROn (Birkbeck, University of London) · Cited by 84
Self-citationThe role of circular dichroism spectroscopy in the era of integrative structural biology
Wallace, B. A. (2019) · Current Opinion in Structural Biology · doi:10.1016/j.sbi.2019.04.001 · Cited by 51
Self-citationAn intrinsically disordered proteins community for ELIXIR
Davey, N. E., Babu, M. M., Blackledge, M. J., Bridge, A. J., Capella-Gutiérrez, S., Dosztányi, Z., Drysdale, R., Edwards, R. J., Elofsson, A., Felli, I. C., et al. (2019) · F1000Research · doi:10.12688/f1000research.20136.1 · Cited by 19
Self-citation
Cited by
Foley, M. H., Walker, M. E., Stewart, A. K., O’Flaherty, S., Gentry, E. C., Patel, S., Beaty, V. V., Allen, G., Pan, M., Simpson, J. B., et al. (2023) · Nature Microbiology · doi:10.1038/s41564-023-01337-7 · Cited by 181
Tiong, A. Y. J., Crawford, S., Jones, N. C., McKinley, G. H., Batchelor, W., & van ’t Hag, L. (2024) · Food Structure · doi:10.1016/j.foostr.2024.100374 · Cited by 49
AlphaDesign: a de novo protein design framework based on AlphaFold
(2025) · doi:10.1038/s44320-025-00119-z · Cited by 36
Han, Z., Song, B., Yang, J., Wang, B., Ma, Z., Yu, L., Li, Y., Xu, H., & Qiao, M. (2022) · Journal of Agricultural and Food Chemistry · doi:10.1021/acs.jafc.2c04668 · Cited by 21
Váradi, G., Bende, G., Borics, A., Dán, K., Rákhely, G., Tóth, G. K., & Galgóczy, L. (2024) · ACS Omega · doi:10.1021/acsomega.3c09377 · Cited by 7
Metadata
- Authors
- Miles, A. J., Ramalli, S. G., & Wallace, B. A.
- Venue
- Protein Science
- Publisher
- Wiley
- Published
- 2021-07-21
- Volume
- 31
- Issue
- 1
- Pages
- 37-46
- ISSN
- 0961-8368 (ISSN-L)
- 1469-896X
- OpenAlex
- W3173650784
- Cited by
- 478
- References
- 32
- FWCI
- 19.59
- Type
- journal article
- Language
- en
- Open access
- hybrid
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review
Data sources
Bibliographic data: Semantic Scholar, OpenAlex, Crossref.
Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.
