Non-covalent interactions reveal the protein chain δ conformation in a flexible single-residue model.
Chem Commun (Camb)
; 59(9): 1161-1164, 2023 Jan 26.
Article
en En
| MEDLINE
| ID: mdl-36625351
The δ conformation is a local secondary structure in proteins that implicates a πamide N-Hâ¯N interaction between a backbone N atom and the NH of the following residue. Small-molecule models thereof have been limited so far to rigid proline-type compounds. We show here that in derivatives of a cyclic amino acid with a sulphur atom in the γ-position, specific side-chain/backbone N-Hâ¯S interactions stabilize the δ conformation sufficiently to allow it to compete with classical C5 and C7 H-bonded conformers.
Texto completo:
1
Colección:
01-internacional
Base de datos:
MEDLINE
Asunto principal:
Proteínas
/
Amidas
Idioma:
En
Revista:
Chem Commun (Camb)
Asunto de la revista:
QUIMICA
Año:
2023
Tipo del documento:
Article
País de afiliación:
Francia
Pais de publicación:
Reino Unido