CD‐resolved secondary structure of bovine plasma albumin in acid‐induced isomerization*

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Abstract
Bovine plasma albumin (BPA) showed the acid‐induced two‐step transition, the N‐F transition and acid‐expansion. Changes in fractions of α‐helix (fα), β‐form (fβ) and unordered form (fR) in the acid‐induced isomerization of BPA were studied using the method of Chen et al. (1972) with two constraints: fi = 1, 0 ± fi ± 1. pH‐profiles of fα and fR showed the two‐step change, one corresponding to the N‐F transition and the other to the acid‐expansion in 0.10 m KCl and in 0.02 m NaClO4. pH‐profile of fβ showed one‐step change, correlating to the later part (lower pH side) of the N‐F transition. The N‐F transition might thus involve the helix ± β and helix ± coil transitions.