Figure 2From: A Method for Structure–Activity Analysis of Quorum-Sensing Signaling Peptides from Naturally Transformable Streptococci Computer-simulated three-dimensional structures of UA159sp and TPC3 determined by NMR and CD analyses. Only the α-helical portions of the peptides with designated hydrophobic and hydrophilic residues are presented. a A comparison in three-dimensional structures between UA159sp (CSP) and TPC3 that lacked the proposed C-terminal motif. b UA159sp viewed from different angles indicates the positions of phenylalanine (F) residues on the core of α-helix and C-terminal motif of slightly motional freedom.Back to article page