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.
