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Three-dimensional structure of a thermophilic family GH11 xylanase from Thermobifida fusca
Thermostable enzymes employ various structural features dictated at the amino-acid sequence level that allow them to maintain their integrity at higher temperatures. Many hypotheses as to the nature of thermal stability have been proposed, including optimized core hydrophobicity and an increase in c...
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| Main Authors: | , , , , |
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| Formato: | Artigo |
| Idioma: | Inglês |
| Publicado em: |
International Union of Crystallography
2012
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| Assuntos: | |
| Acesso em linha: | https://ncbi.nlm.nih.gov/pmc/articles/PMC3274389/ https://ncbi.nlm.nih.gov/pubmed/22297985 https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1107/S1744309111049608 |
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