Table 5.

Correlation between BSA secondary structure and amide I second derivative position ¹.

Secondary Structure	Range, cm−1
α-helix	1650–1660
β-sheet	1628–1639
β-turn	1664–1687
random coil	1640–1649
Intermolecular β-sheet (aggregates)	1618–1626, 1688–1696

¹ Usually, only beta-structures are assigned to multiple bands (e.g., see [54]); expanded ranges for α-helix and random coil peak positions were used as proposed in [55] for albumin.