BeStSel: A web server for accurate protein secondary structure prediction and fold recognition from the circular dichroism spectra

András Micsonai, Frank Wien, Éva Bulyáki, Judit Kun, Éva Moussong, Young Ho Lee, Yuji Goto, Matthieu Réfrégiers, József Kardos

Research output: Contribution to journalArticle

135 Citations (Scopus)

Abstract

Circular dichroism (CD) spectroscopy is a widely used method to study the protein secondary structure. However, for decades, the general opinion was that the correct estimation of β-sheet content is challenging because of the large spectral and structural diversity of β-sheets. Recently, we showed that the orientation and twisting of β-sheets account for the observed spectral diversity, and developed a new method to estimate accurately the secondary structure (PNAS, 112, E3095). BeStSel web server provides the Beta Structure Selection method to analyze the CD spectra recorded by conventional or synchrotron radiation CD equipment. Both normalized and measured data can be uploaded to the server either as a single spectrum or series of spectra. The originality of BeStSel is that it carries out a detailed secondary structure analysis providing information on eight secondary structure components including parallel-β structure and antiparallel β-sheets with three different groups of twist. Based on these, it predicts the protein fold down to the topology/homology level of the CATH protein fold classification. The server also provides a module to analyze the structures deposited in the PDB for BeStSel secondary structure contents in relation to Dictionary of Secondary Structure of Proteins data. The BeStSel server is freely accessible at http://bestsel.elte.hu.

Original languageEnglish
Pages (from-to)W315-W322
JournalNucleic acids research
Volume46
Issue numberW1
DOIs
Publication statusPublished - Jul 2 2018

ASJC Scopus subject areas

  • Genetics

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