Peptide secondary structure prediction and measurement.

<p><b>A</b>. A peptide secondary structure consensus prediction was performed based on the amino acid sequence using a set of online methods, including MLRC, PHD, and SOPM. Each random coil (c), extended strand (e), α helix (h), and ambiguous state (?) corresponded to an amino acid in the peptide sequence. <b>B</b>. The actual secondary structure contents of the peptides were measured by far-ultraviolet (UV) circular dichroism (CD) spectrum. The CD spectra of B28 (dashed line), Bn(6–14) (dot-dashed line) and B28Bn(6–14) (solid line) were recorded in 2 mM sodium phosphate buffer (pH 7.4) at 25°C.