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Enthalpic stabilization of an SH3 domain by D(2)O
The stability of a protein is vital for its biological function, and proper folding is partially driven by intermolecular interactions between protein and water. In many studies, H(2)O is replaced by D(2)O because H(2)O interferes with the protein signal. Even this small perturbation, however, affec...
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| Publicado en: | Protein Sci |
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| Main Authors: | , |
| Formato: | Artigo |
| Idioma: | Inglês |
| Publicado: |
John Wiley & Sons, Inc.
2018
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| Assuntos: | |
| Acceso en liña: | https://ncbi.nlm.nih.gov/pmc/articles/PMC6194290/ https://ncbi.nlm.nih.gov/pubmed/30052291 https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1002/pro.3477 |
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