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Please use this identifier to cite or link to this item: http://dspace.library.iitb.ac.in/jspui/handle/10054/9281

Title: Reengineering a type II beta-turn as a potential helix nucleator-NMR characterization of Boc-Ala-Val-Pro-(D) Asp-Leu-Leu-NHMe
Authors: RAJU, EB
DHANASEKARAN, M
DURANI, S
SRIVASTAVA, S
Keywords: proteins
peptide
conformation
spectra
design
model
water
Issue Date: 2000
Publisher: ISTITUTI EDITORIALI E POLGRAFICI INTERNAZIONALI
Citation: PHYSICA MEDICA, 16(1), 7-11
Abstract: A stereochemically constrained type II beta-turn is reengineered over two steps into a potential helix nucleator. NMR studies in DMSO establish that the hexapeptide Boc-Alal-Val2-Pro3-(D)Asp4-Leu5-Leu6-NHMe is a type II beta-turn at Pro3-(D)Asp4 with a conformation nucleating II-bond between Asp4 carboxylate and Leu6 NH, to which is attributable a type I/III beta-turn at Leu5-Leu6-NHMe potentially capable of serving as a helix template.
URI: http://dspace.library.iitb.ac.in/xmlui/handle/10054/9281
http://hdl.handle.net/10054/9281
ISSN: 1120-1797
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