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Structural Versatility of Peptides from C-Dialkylated Glycines. An Infrared Absorption and H Nuclear Magnetic Resonance Study of Homopeptides from 1-Aminocyclohexane-1-carboxylic Acid

Macromolecules, ISSN: 1520-5835, Vol: 21, Issue: 7, Page: 2071-2074
1988
  • 23
    Citations
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  • 3
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Metric Options:   Counts1 Year3 Year

Metrics Details

  • Citations
    23
    • Citation Indexes
      23
  • Captures
    3

Article Description

The preferred conformation of N- and C-protected homopeptide series of 1-aminocyclohexane-1-carboxylic acid from monomer to pentamer in chloroform solution was determined by using infrared absorption and H nuclear magnetic resonance as a function of concentration, temperature, and addition of perturbing agents. The results obtained are strongly in favor of the onset of an incipient 3 helix at the tripeptide level, as found in the crystal state. A comparison is also made with the conformational propensities of homopeptides of 1-aminocyclopentane-1-carboxylic acid and the C-dialkylated glycyl residues with linear side chains. © 1988, American Chemical Society. All rights reserved.

Bibliographic Details

M. Crisma; G. M. Bonora; C. Toniolo; A. Bavoso; E. Benedetti; B. Di Blasio; V. Pavone; C. Pedone

American Chemical Society (ACS)

Chemistry; Materials Science

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