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Citations per year

Number of citations per year for the bioinformatics software tool BeStSel

Tool usage distribution map

This map represents all the scientific publications referring to BeStSel per scientific context
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BeStSel specifications


Unique identifier OMICS_12757
Name BeStSel
Alternative name Beta Structure Selection
Interface Web user interface
Restrictions to use None
Input data Wavelength and CD data
Computer skills Basic
Stability Stable
Maintained Yes


  • person_outline József Kardos

Publications for Beta Structure Selection

BeStSel citations


Ehrlichia chaffeensis TRP120 nucleomodulin binds DNA with disordered tandem repeat domain

PLoS One
PMCID: 5895000
PMID: 29641592
DOI: 10.1371/journal.pone.0194891

[…] θ] is the molar residue ellipticity, θ is the CD signal in millidegrees, c is the protein concentration in μM, l is the pathlength in mm, and n is the number of residues. The CD data analysis program BestSel was used to analyze the data and estimate the secondary structure []. […]


The C‐terminal cytosolic domain of the human zinc transporter ZnT8 and its diabetes risk variant

PMCID: 5947572
PMID: 29430817
DOI: 10.1111/febs.14402

[…] or all spectra, the protein concentrations were 0.2 mg·mL−1 in 10 mm potassium phosphate, pH 8, 60 mm NaCl, 20 mm sucrose. Protein secondary structure content based on CD spectra was determined using BeStSel . Melting analyses involved monitoring the CD signal at 222 nm between 6 and 92 °C at a heating rate of 1 °C·min−1. Separate far‐UV spectra and melting analyses were performed with both varian […]


Influence of solubilization and AD mutations on stability and structure of human presenilins

Sci Rep
PMCID: 5740079
PMID: 29269939
DOI: 10.1038/s41598-017-18313-x

[…] y was accessed by triplicate measurement (see Supplementary Figure ). The influence of the deconvolution algorithm was monitored by processing the data by CDSSTR, (with reference data set SMP180) and BeStSel (see Supplementary Figure ).Tryptophan fluorescence emission spectra (450 to 310 nm with wavelength steps of 1 nm, an excitation wavelength of 295 nm, a bandwidth of 2 nm, a PMT voltage of 900 […]


Co(II) Coordination in Prokaryotic Zinc Finger Domains as Revealed by UV Vis Spectroscopy

PMCID: 5745721
PMID: 29386985
DOI: 10.1155/2017/1527247

[…] aracteristic of well-structured proteins containing both α-helical and β-sheet secondary structure. We estimated from the CD data the protein secondary structure for the two proteins using the server BeStSel (Figures and ). This server fits the CD experimental curve by linearly combining fixed basis components to get the percentage of the eight secondary structural elements []. The data indicate […]


Quantification of the catalytic performance of C1 cellulose specific lytic polysaccharide monooxygenases

Appl Microbiol Biotechnol
PMCID: 5778151
PMID: 29196788
DOI: 10.1007/s00253-017-8541-9

[…] pectra recorded at 20 °C (Fig. a, b) revealed that both MtLPMOs share a high content of antiparallel β-sheets, whereas the content of α-helices and β-turns is relatively low (Supplemental Fig. ). The BeStSel method was used because it has been reported to be a reliable tool for the estimation of the secondary structure composition (%) of proteins which contain high amounts of β-structures (Micsona […]


Large scale in vitro production, refolding and dimerization of PsbS in different microenvironments

Sci Rep
PMCID: 5680255
PMID: 29123155
DOI: 10.1038/s41598-017-15068-3

[…] e secondary folds of the refolded PsbS were analyzed by UV CD spectroscopy (Jasco J-815) using step size of 1 sec/nm, bandwidth of 1 nm and a scanning speed 100 nm/min. CD spectra were analyzed using BeStSel (Beta Structure Selection) for estimating the content of α-helical, beta sheet and coil or other conformations for each CD spectrum. […]

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BeStSel institution(s)
Department of Biochemistry and MTA-ELTE NAP B Neuroimmunology Research Group, Institute of Biology, Eötvös Loránd University, Budapest, Hungary; DISCO Beamline, Synchrotron SOLEIL, Gif-sur-Yvette, France; Division of Protein Structural Biology, Institute for Protein Research, Osaka University, Osaka, Japan
BeStSel funding source(s)
This work was supported by the Hungarian Scientific Research Fund (K81950) and KTIA_NAP_13-2-2014-0017. SRCD measurements were supported by SOLEIL (Proposals 20140646, 20130475, 20120589, 201110054, and 20110405).

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