Tailoring protein nanomechanics with chemical reactivity
Post-translational modifications modulate nanomechanics of proteins. Here the authors use single-molecule force-clamp spectroscopy supported by density functional theory calculations to show how reactive low-weight molecular thiol compounds directly affect mechanical protein folding.
Guardado en:
Autores principales: | Amy E. M. Beedle, Marc Mora, Steven Lynham, Guillaume Stirnemann, Sergi Garcia-Manyes |
---|---|
Formato: | article |
Lenguaje: | EN |
Publicado: |
Nature Portfolio
2017
|
Materias: | |
Acceso en línea: | https://doaj.org/article/7f39aa321a0a4c9e85b067804b4cb304 |
Etiquetas: |
Agregar Etiqueta
Sin Etiquetas, Sea el primero en etiquetar este registro!
|
Ejemplares similares
-
Protein S-sulfenylation is a fleeting molecular switch that regulates non-enzymatic oxidative folding
por: Amy E. M. Beedle, et al.
Publicado: (2016) -
Forcing the reversibility of a mechanochemical reaction
por: Amy E. M. Beedle, et al.
Publicado: (2018) -
Engineered Ureolytic Microorganisms Can Tailor the Morphology and Nanomechanical Properties of Microbial-Precipitated Calcium Carbonate
por: Chelsea M. Heveran, et al.
Publicado: (2019) -
Nanomechanics of individual aerographite tetrapods
por: Raimonds Meija, et al.
Publicado: (2017) -
Single-particle mass spectrometry with arrays of frequency-addressed nanomechanical resonators
por: Eric Sage, et al.
Publicado: (2018)