Comment on “N-terminal Protein Tail Acts as Aggregation Protective Entropic Bristles: The SUMO Case”

SUMO-2
protein, SUMO-2 core domain, and the tail peptide corresponding
to the first 14 residues were produced by chemical synthesis, and
their secondary structures were analyzed by circular dichroism. The
CD spectra of SUMO-2 and SUMO-2 core domain show distinct features
and α-helical contents. In particular, the presence of the disordered
tail in SUMO-2 lowers the α-helical content of the protein compared
with SUMO-2 core domain and also explains the shift in the position
of the minimum around 208 nm.