1568826-40-3Relevant academic research and scientific papers
Conformational modulation of peptide secondary structures using β-aminobenzenesulfonic acid
Kale, Sangram S.,Kunjir, Shrikant M.,Gawade, Rupesh L.,Puranik, Vedavati G.,Rajamohanan,Sanjayan, Gangadhar J.
supporting information, p. 2886 - 2888 (2014/03/21)
This communication describes the influence of β-aminobenzenesulfonic acid (SAnt) on the conformational preferences of hetero foldamers. The designed (Aib-SAnt-Aib)n and (Aib-SAnt-Pro) n oligomers display a well-defined folded conformation featuring intramolecular mixed hydrogen bonding (7/11) and intra-residual (6/5) H-bonding interactions, respectively.
