95863-98-2Relevant articles and documents
Design of peptides with α,β-dehydro residues: A dipeptide with a branched β-carbon dehydro residue at the (i+1) position, methyl N-(benzyloxycarbonyl)-α, β-didehydrovalyl-l-tryptophanate
Vijayaraghavan,Kumar,Dey,Singh
, p. 1220 - 1221 (2001)
The structure of the title peptide, C25H27N3O5, has been determined and its conformation analysed. Values of the standard peptide torsion angles are Φ1 = -44.2 (3)°, Ψ1 = 135.9 (2)°, Φ
Impact of Dehydroamino Acids on the Structure and Stability of Incipient 310-Helical Peptides
Joaquin, Daniel,Lee, Michael A.,Kastner, David W.,Singh, Jatinder,Morrill, Shardon T.,Damstedt, Gracie,Castle, Steven L.
, p. 1601 - 1613 (2019/12/02)
A comparative study of the impact of small, medium-sized, and bulky α,β-dehydroamino acids (AAs) on the structure and stability of Balaram's incipient 310-helical peptide (1) is reported. Replacement of the N-terminal Aib residue of 1 with a AA
Design of peptides with α,β-dehydro-residues: Synthesis, crystal structure and molecular conformation of a tetrapeptide Z-ΔVal-Val-ΔPhe-Ile-Ome
Makker,Dey,Mukherjee,Vijayaraghavan,Kumar,Singh
, p. 119 - 124 (2007/10/03)
This is the first designed peptide with a combination of a branched β-carbon ΔVal and a ΔPhe residues. The peptide Z-ΔVal-Val-ΔPhe-Ile-Ome was synthesized in solution phase. Single crystals were grown by slow evaporation from its solution in acetone-water
