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

Micsonai, András and Wien, F. and Bulyáki, Éva and Kun, J. and Moussong, E. and Kardos, József (2018) BeStSel: a web server for accurate protein secondary structure prediction and fold recognition from the circular dichroism spectra. NUCLEIC ACIDS RESEARCH, 46 (W1). W315-W322. ISSN 0305-1048

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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 beta-sheet content is challenging because of the large spectral and structural diversity of beta-sheets. Recently, we showed that the orientation and twisting of beta-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-beta structure and antiparallel beta-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.

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