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 |
- *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.