On the role of entropy in the stabilization of α-Helixes
Ver/
Compartir
Estadísticas
Ver Estadísticas de usoMetadatos
Mostrar el registro completo del ítemAutor
Bastida Pascual, Adolfo; Zúñiga Román, José; Requena Rodríguez, Alberto; Miguel Hernández, Beatriz; Cerezo Bastida, JavierÁrea de conocimiento
Ingeniería QuímicaPatrocinadores
This work was partially supported by the Spanish Agencia Estatal de Investigación (AEI) and Fondo Europeo de Desarrollo Regional (FEDER, UE) under Project CTQ2016-79345-P and by the Fundación Séeneca under Project 20789/PI/18. We thank the computational assistance provided by J. F. Hidalgo of the Servicio de Infraestructuras TIC de ATICA.Fecha de publicación
2020Editorial
American Chemical SocietyCita bibliográfica
Bastida A., Zúñiga J., Requena A., Miguel B., Cerezo J. On the Role of Entropy in the Stabilization of α-Helices. Journal of Chemical Information and Modeling. 2020 Dec;60(12):6523-6531. DOI: 10.1021/acs.jcim.0c01177.Palabras clave
EntropyFree energy
Peptides and proteins
Molecules
Conformation
Resumen
Protein folding evolves by exploring the conformational space with a subtle balance between enthalpy and entropy changes which eventually leads to a decrease of free energy upon reaching the folded structure. A complete understanding of this process requires, therefore, a deep insight into both contributions to free energy. In this work, we clarify the role of entropy in favoring the stabilization of folded structures in polyalanine peptides with up to 12 residues. We use a novel method referred to as K2V that allows us to obtain the potential-energy landscapes in terms of residue conformations extracted from molecular dynamics simulations at conformational equilibrium and yields folding thermodynamic magnitudes, which are in agreement with the experimental data available. Our results demonstrate that the folded structures of the larger polyalanine chains are stabilized with respect to the folded structures of the shorter chains by both an energetic contribution coming from the formation ...
Colecciones
- Artículos [1733]
El ítem tiene asociados los siguientes ficheros de licencia:
Redes sociales