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The Pro‐Gly motif is often involved in protein–protein interactions and may participate in intracellular signalling cascades. Conformationally constrained short protein‐derived turn peptides thus offer promise for the development of drug candidates that could interfere with these interactions. Byrne et al. report ECD and NMR spectroscopy studies, as well as molecular dynamics simulations, that show the short 363–367 peptide motif of the human oestrogen receptor α (RVPGF) adopts a type II β-turn around the trans Pro-Gly motif. When the proline is substituted by a 5,5- dimethylproline, a cis isomer adopting a type VIb β-turn centred on the Val-Pro segment is detected. (doi: 10.1002/pep2.24113) EDITOR-IN-CHIEF P. Balaram Gregg B. Fields Yong-beom Lim Fred Naider Indian Institute of Florida Atlantic Yonsei University College of Staten Island Hilary J. Crichton Science University Seoul, South Korea Staten Island, NY, U.S.A. Bangalore, India Boca Raton, FL, U.S.A. ASSOCIATE EDITOR Robin Offord George Barany Shiroh Futaki William D. Lubell Conor H. Doss The Mintaka University of Minnesota Kyoto University Université de Montréal Foundation for Medical Minneapolis, MN, U.S.A. Kyoto, Japan Montréal, Canada Research EXECUTIVE EDITORS Plan-les-Ouates, Annette G. Samuel H. Gellman Joel P. Schneider Switzerland Beck-Sickinger Radhakrishnan University of Wisconsin- Frederick, MD, U.S.A. University of Leipzig
Peptide Science – Wiley
Published: Jul 1, 2019
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