Chiral effects on helicity studied via the energy landscape of short (D, L)-alanine peptides.
J Chem Phys
; 143(16): 165103, 2015 Oct 28.
Article
en En
| MEDLINE
| ID: mdl-26520555
The homochirality of natural amino acids facilitates the formation of regular secondary structures such as α-helices and ß-sheets. Here, we study the relationship between chirality and backbone structure for the example of hexa-alanine. The most stable stereoisomers are identified through global optimisation. Further, the energy landscape, a database of connected low-energy local minima and transition points, is constructed for various neutral and zwitterionic stereoisomers of hexa-alanine. Three order parameters for partial helicity are applied and metric disconnectivity graphs are presented with partial helicity as a metric. We also apply the Zimm-Bragg model to derive average partial helicities for Ace-(L-Ala)6-NHMe, Ace-(D-Ala-L-Ala)3-NHMe, and Ace-(L-Ala)3-(D-Ala)3-NHMe from the database of local minima and compare with previous studies.
Texto completo:
1
Colección:
01-internacional
Base de datos:
MEDLINE
Asunto principal:
Oligopéptidos
/
Alanina
Idioma:
En
Revista:
J Chem Phys
Año:
2015
Tipo del documento:
Article
País de afiliación:
Reino Unido
Pais de publicación:
Estados Unidos