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
- 23Citations
- 3Captures
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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.
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