Residual secondary structure occurs frequently in IDPs, and a quick browsing of the BMRB benchmark used by the authors shows that BMRB ID 11526 has nearly significant alpha-helical secondary structure between residues ~60-78, reaching a maximum value of ~50% near residue 70 ( https://link.springer.com/article/10.1007/s12104-013-9523-1 ).
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Linear discriminant analysis reveals hidden patterns in NMR chemical shifts of intrinsically disordered proteins.
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