Sequence-specific destabilization of azurin by tetramethylguanidinium-dipeptide ionic liquids

The thermal unfolding of the copper redox protein azurin was studied in the presence of four different dipeptide-based ionic liquids (ILs) utilizing tetramethylguanidinium as the cation. The four dipeptides have different sequences including the amino acids Ser and Asp: TMG-AspAsp, TMG-SerSer, TMG-S...

Descripción completa

Detalles Bibliográficos
Autores principales: Patel, Roshani, Clark, Austin K., DeStefano, Gabriella, DeStefano, Isabella, Gogoj, Hunter, Gray, Erin, Patel, Aashka Y., Hauner, Joshua T., Caputo, Gregory A., Vaden, Timothy D.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Elsevier 2022
Materias:
Research Article
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8907678/
https://www.ncbi.nlm.nih.gov/pubmed/35280523
http://dx.doi.org/10.1016/j.bbrep.2022.101242

Internet

https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8907678/
https://www.ncbi.nlm.nih.gov/pubmed/35280523
http://dx.doi.org/10.1016/j.bbrep.2022.101242

Ejemplares similares