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 solid-state conformation of (αMe)Trp peptides
✍ Scribed by FORMAGGIO, F. ;TONIOLO, C. ;CRISMA, M. ;VALLE, G. ;KAPTEIN, B. ;SCHOEMAKER, H.E. ;KAMPHUIS, J. ;BLASIO, B. ;MAGLIO, O. ;FATTORUSSO, R. ;BENEDETTI, E. ;SANTINI, A.
- Book ID
- 115099838
- Publisher
- Wiley (Blackwell Publishing)
- Year
- 2009
- Tongue
- English
- Weight
- 666 KB
- Volume
- 45
- Category
- Article
- ISSN
- 0367-8377
No coin nor oath required. For personal study only.
📜 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 molecular structures of four protected isovaline-(Iva-)containing peptides to the pentamer level have been determined by x-ray diffraction. The peptides are t-Boc-Ala-( S ) -1va-Ala-OMe ( t-Boc : tert-butyloxycarbonyl; OMe : methoxy) and its ( R ) -1va diastereomer, and t-Boc-[ Ala-( R ) -Iva],-