## Abstract Our previous studies of the potential utility of the C^α^D^α^ stretch frequency, ν(CD), as a tool for determining conformation in peptide systems (Mirkin and Krimm, J Phys Chem A 2004, 108, 10923–10924; 2007, 111, 5300–5303) dealt with the spectroscopic characteristics of isolated alani
Conformation Dependence of the C α D α Stretch Mode in Peptides. 1. Isolated Alanine Peptide Structures
✍ Scribed by Mirkin, Noemi G.; Krimm, Samuel
- Book ID
- 126118435
- Publisher
- American Chemical Society
- Year
- 2007
- Tongue
- English
- Weight
- 54 KB
- Volume
- 111
- Category
- Article
- ISSN
- 1089-5639
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## Abstract We use the nmr data concerning the C^α^HC^β^H fragment in eight peptides with rigid side chains to parametrize a Karplus correlation between the vicinal proton __J__~αβ~ coupling constant and the dihedral angle θ. When considering molecules containing the fragment C^α^H^α^C^β^H^β^H^β′
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