The DOI matches its Crossref record; 4 of the 4 references it cites were found in a registry or an index.
BeStSel: webserver for secondary structure and fold prediction for protein CD spectroscopy
Open accessAbstract
Circular dichroism (CD) spectroscopy is widely used to characterize the secondary structure composition of proteins. To derive accurate and detailed structural information from the CD spectra, we have developed the Beta Structure Selection (BeStSel) method (PNAS, 112, E3095), which can handle the spectral diversity of β-structured proteins. The BeStSel webserver provides this method with useful accessories to the community with the main goal to analyze single or multiple protein CD spectra. Uniquely, BeStSel provides information on eight secondary structure components including parallel β-structure and antiparallel β-sheets with three different groups of twist. It overperforms any available method in accuracy and information content, moreover, it is capable of predicting the protein fold down to the topology/homology level of the CATH classification. A new module of the webserver helps to distinguish intrinsically disordered proteins by their CD spectrum. Secondary structure calculation for uploaded PDB files will help the experimental verification of protein MD and in silico modelling using CD spectroscopy. The server also calculates extinction coefficients from the primary sequence for CD users to determine the accurate protein concentrations which is a prerequisite for reliable secondary structure determination. The BeStSel server can be freely accessed at https://bestsel.elte.hu.
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Cites
Highly accurate protein structure prediction with AlphaFold
Jumper, J., Evans, R., Pritzel, A., Green, T., Figurnov, M., Ronneberger, O., Tunyasuvunakool, K., Bates, R., Žídek, A., Potapenko, A., et al. (2021) · Nature · doi:10.1038/s41586-021-03819-2 · Cited by 43,764
Kabsch, W., & Sander, C. (1983) · Biopolymers · doi:10.1002/bip.360221211 · Cited by 15,320
Introduction to Information Retrieval
Manning, C. D., Raghavan, P., & Schütze, H. (2008) · doi:10.1017/cbo9780511809071 · Cited by 11,288
Highly accurate protein structure prediction for the human proteome
Tunyasuvunakool, K., Adler, J., Wu, Z., Green, T., Zielinski, M., Žídek, A., Bridgland, A., Cowie, A., Meyer, C., Laydon, A., et al. (2021) · Nature · doi:10.1038/s41586-021-03828-1 · Cited by 3,025 · cited 2×
“This is crucial for the experimental verification of MD simulation results or in silico models, such as AlphaFold2 (42) structures, making the structural comparison with the results of CD spectrum analysis possible.”
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Borrelia burgdorferi PlzA is a cyclic‐di‐GMP dependent DNA and RNA binding protein
Jusufovic, N., Krusenstjerna, A. C., Savage, C. R., Saylor, T. C., Brissette, C. A., Zückert, W. R., Schlax, P. J., Motaleb, M. A., & Stevenson, B. (2024) · Molecular Microbiology · doi:10.1111/mmi.15254 · Cited by 7
Intrinsic Disorder of the Neuronal SNARE Protein SNAP25a in its Pre-fusion Conformation
Stief, T., Gremer, L., Pribicevic, S., Espinueva, D. F., Vormann, K., Biehl, R., Jahn, R., Pérez-Lara, Á., & Lakomek, N.-A. (2023) · Journal of Molecular Biology · doi:10.1016/j.jmb.2023.168069 · Cited by 6
The potent PHL4 transcription factor effector domain contains significant disorder
Fonda, B. D., & Murray, D. T. (2024) · Protein Science · doi:10.1002/pro.5214 · Cited by 1
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Metadata
- Authors
- Micsonai, A., Moussong, É., Wien, F., Boros, E., Vadászi, H., Murvai, N., Lee, Y.-H., Molnár, T., Réfrégiers, M., Goto, Y., Tantos, Á., & Kardos, J.
- Venue
- Nucleic Acids Research
- Publisher
- Oxford University Press (OUP)
- Published
- 2022-05-11
- Volume
- 50
- Issue
- W1
- Pages
- W90-W98
- ISSN
- 0305-1048 (ISSN-L)
- 1362-4962
- OpenAlex
- W4280502047
- Cited by
- 455
- References
- 4
- FWCI
- 25.14
- Type
- journal article
- Language
- en
- Open access
- gold
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