## Abstract The preferred conformation of five, terminally protected, model peptide series to the hexamer level, based on three novel crowned, C^α^‐methyl L‐DOPA amino acids combined with either L‐Ala/Aib or Gly/Aib, were assessed in structure supporting solvents using FT‐IR absorption, ^1^H NMR, a
New tools for the control of peptide conformation: the helicogenic Cα-methyl, Cα-cyclohexylglycine*
✍ Scribed by Formaggio, F. ;Moretto, V. ;Crisma, M. ;Toniolo, C. ;Kaptein, B. ;Broxterman, Q.B.
- Book ID
- 110893744
- Publisher
- John Wiley and Sons
- Year
- 2004
- Tongue
- English
- Weight
- 375 KB
- Volume
- 63
- Category
- Article
- ISSN
- 1397-002X
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📜 SIMILAR VOLUMES
## Abstract The preferred conformation of the C^α,α^‐diphenylglycine residue was determined in simple derivatives and dipeptides. The dipeptides were synthesized by the 5(4__H__)‐oxazolone (from the N‐__para__‐bromobenzoylated amino acid) method. This activated intermediate and a reaction by‐produc
The lipophilic, chiral, C h -methylated h-amino acid L-(h Me)Aoc (2-methyl-2-amino-octanoic acid) was prepared using a chemo-enzymatic approach. Two series of terminally protected model peptides, from dimer through to hexamer, containing L-(h Me)Aoc in combination with either Gly or Aib, were synthe
The preferred conformations of C"-methyl phenylglycine, C"-methyl phenylalanine, and C"-methyl homophenylalanine residues, as determined in model peptides (including homopeptides) by Fourier transform ir absorption, 'H-nmr, CD, and x-ray diffraction techniques, are compared with the aim of investiga