01540nas a2200181   4500008004100000022001400041245006500055210006300120260011000183300001600293490000700309520084400316100002101160700002501181700002401206700002801230856010001258       2014                        eng d  a1359-734500aSynthetic turn mimetics and hairpin nucleators: quo vadimus?0 aSynthetic turn mimetics and hairpin nucleators quo vadimus  aTHOMAS GRAHAM HOUSE, SCIENCE PARK, MILTON RD, CAMBRIDGE CB4 0WF, CAMBS, ENGLANDbROYAL SOC CHEMISTRYcOCT  a13874-138840 v503 a<p>Structural mimicry of peptides has witnessed perceptible progress in the last three decades. Reverse turn and beta-hairpin units are the smallest secondary structural motifs that are some of the most scrutinized functional cores of peptides and proteins. The practice of mimicking, without altering the function of the bioactive core, ranges from conformational locking of the basic skeleton to total replacement of structural architecture using synthetic analogues. Development of heterogeneous backbones - using unnatural residues in place of natural ones - has broadened further opportunities for efficient structural rigidification. This feature article endeavours to trail the path of progress achieved hitherto and envisage the possibilities that lie ahead in the development of synthetic turn mimetics and hairpin nucleators.</p>1 aNair, Roshna, V.1 aBaravkar, Sachin, B.1 aIngole, Tukaram, S.1 aSanjayan, Gangadhar, J.  uhttps://library.ncl.res.in/content/synthetic-turn-mimetics-and-hairpin-nucleators-quo-vadimus-0