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Origins of the high 14-helix propensity of cyclohexyl-rigidified residues in β-peptides

Lee, MR and Raguse, TL and Schinnerl, M and Pomerantz, WC and Wang, X and Wipf, P and Gellman, SH (2007) Origins of the high 14-helix propensity of cyclohexyl-rigidified residues in β-peptides. Organic Letters, 9 (9). 1801 - 1804. ISSN 1523-7060

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Abstract

β-Peptides containing residues derived from trans-2- aminocyclohexanecarboxylic acid (ACHC) display high population of 14-helical secondary structure in aqueous solution. We show that hydrophobic interactions between cyclohexyl rings are not responsible for this conformationpromoting effect, and that polar groups may be attached to the cyclohexyl ring without diminishing the effect. © 2007 American Chemical Society.


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Details

Item Type: Article
Status: Published
Creators/Authors:
CreatorsEmailPitt UsernameORCID
Lee, MR
Raguse, TL
Schinnerl, M
Pomerantz, WC
Wang, X
Wipf, Ppwipf@pitt.eduPWIPF
Gellman, SH
Date: 26 April 2007
Date Type: Publication
Journal or Publication Title: Organic Letters
Volume: 9
Number: 9
Page Range: 1801 - 1804
DOI or Unique Handle: 10.1021/ol070511r
Schools and Programs: Dietrich School of Arts and Sciences > Chemistry
Refereed: Yes
ISSN: 1523-7060
MeSH Headings: Circular Dichroism; Cyclization; Magnetic Resonance Spectroscopy; Peptides--chemistry; Protein Structure, Secondary
PubMed ID: 17394351
Date Deposited: 09 Oct 2013 15:50
Last Modified: 05 Feb 2019 16:55
URI: http://d-scholarship.pitt.edu/id/eprint/19809

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