The conformational preferences of the alicyclic C","-disubstituted glycines Ac,c (I-amino-I-cycloalkane-carboxylic acid; n = 4 , 7, 9, 1 2 ) were assessed in selected model compounds, including homopeptides and Ala (or Aib, a-aminoisobutyric acid)lAc,c peptides containing a small total number of res
Intrinsic Conformational Preferences of C α,α -Dibenzylglycine
✍ Scribed by Casanovas, Jordi; Nussinov, Ruth; Alemán, Carlos
- Book ID
- 127396191
- Publisher
- American Chemical Society
- Year
- 2008
- Tongue
- English
- Weight
- 763 KB
- Volume
- 73
- Category
- Article
- ISSN
- 0022-3263
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## 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
## Abstract The conformational preference of C^α,α^‐diphenylglycinc (Døg) and C^α,α^‐dibenzylglycine (Dbz) residues was assessed in selected derivatives and small peptides by conformational energy computations, ir absorption, ^1^H‐nmr, and x‐ray diffraction. Conformational energy computations on th
The conformational preferences of linear peptides containing a,a-disubstituted a-amino acids, derived from the crystal structures of 28 compounds, are reviewed. In particular, the sensitivity of peptide conformation to the geometry of these unusual amino acids is underlined. We also consider possibl