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A Method for Assessing the Robustness of Protein Structures by Randomizing Packing Interactions
Many single-domain proteins are not only stable and water-soluble, but they also populate few to no intermediates during folding. This reduces interactions between partially folded proteins, misfolding, and aggregation, and makes the proteins tractable in biotechnological applications. Natural prote...
| Autores principales: | , , |
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| Formato: | Online Artículo Texto |
| Lenguaje: | English |
| Publicado: |
Frontiers Media S.A.
2022
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| Materias: | |
| Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9271847/ https://www.ncbi.nlm.nih.gov/pubmed/35832734 http://dx.doi.org/10.3389/fmolb.2022.849272 |