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Characterization of conformational heterogeneity via higher-dimensionality, proton-detected solid-state NMR
Site-specific heterogeneity of solid protein samples can be exploited as valuable information to answer biological questions ranging from thermodynamic properties determining fibril formation to protein folding and conformational stability upon stress. In particular, for proteins of increasing molec...
| Autores principales: | , , |
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| Formato: | Online Artículo Texto |
| Lenguaje: | English |
| Publicado: |
Springer Netherlands
2022
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| Materias: | |
| Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9712413/ https://www.ncbi.nlm.nih.gov/pubmed/36149571 http://dx.doi.org/10.1007/s10858-022-00405-0 |