Cargando…
Probing the folding of mini-protein Beta3s by two-dimensional infrared spectroscopy; simulation study
We propose to use infrared coherent two-dimensional correlation spectroscopy (2DCS) to characterize the folding mechanism of the mini-protein Beta3s. In this study Beta3s was folded by molecular dynamics (MD) simulation and intermediate conformational ensembles were identified. The one and two-dimen...
Autores principales: | Marai, Christopher NJ, Mukamel, Shaul, Wang, Jin |
---|---|
Formato: | Texto |
Lenguaje: | English |
Publicado: |
BioMed Central
2010
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2851665/ https://www.ncbi.nlm.nih.gov/pubmed/20302645 http://dx.doi.org/10.1186/1757-5036-3-8 |
Ejemplares similares
-
Signatures
of the Protein Folding Pathway in Two-Dimensional
Ultraviolet Spectroscopy
por: Jiang, Jun, et al.
Publicado: (2014) -
Disentangling
Peptide Configurations via Two-Dimensional
Electronic Spectroscopy: Ab Initio Simulations Beyond the Frenkel
Exciton Hamiltonian
por: Nenov, Artur, et al.
Publicado: (2014) -
Two-dimensional x-ray correlation spectroscopy of remote core states
por: Healion, Daniel, et al.
Publicado: (2013) -
Photoinduced molecular chirality probed by ultrafast resonant X-ray spectroscopy
por: Rouxel, Jérémy R., et al.
Publicado: (2017) -
Two-dimensional infrared-Raman spectroscopy as a probe of water’s tetrahedrality
por: Begušić, Tomislav, et al.
Publicado: (2023)