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Selection and analyses of variants of a designed protein suggest importance of hydrophobicity of partially buried sidechains for protein stability at high temperatures
Computationally designed proteins of high stability provide specimen in addition to natural proteins for the study of sequence‐structure stability relationships at the very high end of protein stability spectrum. The melting temperature of E_1r26, a protein we previously designed using the A Backbon...
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| Publicado en: | Protein Sci |
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| Main Authors: | , , , , , |
| Formato: | Artigo |
| Idioma: | Inglês |
| Publicado: |
John Wiley & Sons, Inc.
2019
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| Assuntos: | |
| Acceso en liña: | https://ncbi.nlm.nih.gov/pmc/articles/PMC6635770/ https://ncbi.nlm.nih.gov/pubmed/31074908 https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1002/pro.3643 |
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