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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Item Type: |
Article
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Status: |
Published |
Creators/Authors: |
Creators | Email | Pitt Username | ORCID ![](/images/orcid_id_24x24.png) |
---|
Lee, MR | | | | Raguse, TL | | | | Schinnerl, M | | | | Pomerantz, WC | | | | Wang, X | | | | Wipf, P | pwipf@pitt.edu | PWIPF | | Gellman, SH | | | |
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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-dev.library.pitt.edu/id/eprint/19809 |
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