FraC nanopores with adjustable diameter identify the mass of opposite-charge peptides with 44 dalton resolution
Using Fragaceatoxin C nanopores to study peptides below 1.6 kDa is challenging. Here the authors demonstrate that nanopores can be engineered to different sizes to detect a range of peptide lengths below the previous resolution limit, and show that the mass of a peptide can be identified by ionic cu...
Guardado en:
| Autores principales: | , , |
|---|---|
| Formato: | article |
| Lenguaje: | EN |
| Publicado: |
Nature Portfolio
2019
|
| Materias: | |
| Acceso en línea: | https://doaj.org/article/09dd1600d7044d409d1462d825c5945f |
| Etiquetas: |
Agregar Etiqueta
Sin Etiquetas, Sea el primero en etiquetar este registro!
|
| Sumario: | Using Fragaceatoxin C nanopores to study peptides below 1.6 kDa is challenging. Here the authors demonstrate that nanopores can be engineered to different sizes to detect a range of peptide lengths below the previous resolution limit, and show that the mass of a peptide can be identified by ionic current blockades. |
|---|