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Table 3 Proportions of secondary structure in micelles for PC-72 and PC-73 from FTIR spectra and molecular dynamics simulations*. Data are the mean of 5 separate determinations.

From: Comparison of interactions between beta-hairpin decapeptides and SDS/DPC micelles from experimental and simulation data

Sample % Beta sheet %Loop-turn %Disordered %Helix
PC-72 SDS FTIR 43.3 42.3 4.4 10.0
PC-72 SDS Simulation 52.0 27.2 14.4 6.4
PC-72 DPC FTIR 54.0 30.8 10.2 5.0
PC-72 DPC Simulation 54.2 27.4 9.3 9.1
PC-73 SDS FTIR 23.4 48.1 18.5 10.0
PC-73 SDS Simulation 40.0 29.0 20.0 11.0
PC-73 DPC FTIR 38.6 46.1 6.3 9.0
PC-73 DPC Simulation 43.0 27.0 15.0 15.0
  1. *The percentage residue specific anti-parallel and parallel beta sheet conformations were determined from peptide simulation structures using the Hyperchem 7.5 secondary structure analysis utility. This utility classifies anti-parallel beta sheet as residues having dihedral angles of Φ = -139° and ψ = 135° and parallel beta sheet as residues having dihedral angles of Φ = -119° and ψ = 113°. The values in the above table represent the sum of residues participating in anti-parallel and parallel beta sheet structures for a given peptide in a specific environment. Similar analysis procedures were used for helix and random conformations. Loop structure percentages were based on the residues participating in disulfide stabilized loop sequence since there is no specific secondary structure classification for this motif in the analysis utility.