Backbone regulation mimicry by β-peptidic foldamers: Formation of a 10-helix in a mixed 6-strand/14-helix conformational pool

Jagadeesh, Bharatam ; Udaya Kiran, Marelli ; Sudhakar, Ambadi ; Chandrasekhar, Srivari (2009) Backbone regulation mimicry by β-peptidic foldamers: Formation of a 10-helix in a mixed 6-strand/14-helix conformational pool Chemistry - A European Journal, 15 (46). 1259q-12595. ISSN 0947-6539

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Official URL: http://onlinelibrary.wiley.com/doi/10.1002/chem.20...

Related URL: http://dx.doi.org/10.1002/chem.200902332

Abstract

Hybrid β-peptide foldamer: Detailed NMR spectroscopy studies have revealed the formation of a new class of 10-helix in hybrid β-peptidic assembly comprised of 6-strand and 14-helical nucleating motifs. These findings show a new means of accessing intermediate secondary structures and also mimic backbone regulations in biomolecules.

Item Type:Article
Source:Copyright of this article belongs to John Wiley and Sons.
Keywords:Beta Peptides; Helical Structures; Backbone Regulation; Hybrid Conformation; NMR Spectroscopy; Peptides
ID Code:62340
Deposited On:22 Sep 2011 03:36
Last Modified:22 Sep 2011 03:36

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