The serine-proline turn: a novel hydrogen-bonded template for designing peptidomimetics.
Org Lett
; 14(3): 732-5, 2012 Feb 03.
Article
en En
| MEDLINE
| ID: mdl-22257322
ABSTRACT
Serine-Proline (SP) dipeptide motifs have been shown to form unique hydrogen-bonding patterns in protein crystal structures. Peptides were designed to mimic these patterns by forming the 6 + 10 and the 9 + 10 hydrogen-bonded rings. Factors that contribute to the formation of SP turns include controlling backbone flexibility and amino acid chirality along with creating a hydrophobic environment around the intramolecular hydrogen bonds.
Texto completo:
1
Colección:
01-internacional
Banco de datos:
MEDLINE
Asunto principal:
Peptidomiméticos
Tipo de estudio:
Prognostic_studies
Idioma:
En
Revista:
Org Lett
Asunto de la revista:
BIOQUIMICA
Año:
2012
Tipo del documento:
Article
País de afiliación:
Estados Unidos