Role of residual structure in the unfolded state of a thermophilic protein
Ribonucleases H from the thermophilic bacterium Thermus thermophilus and the mesophile Escherichia coli demonstrate a dramatic and surprising difference in their change in heat capacity upon unfolding (ΔCp°). The lower ΔCp° of the thermophilic protein directly contributes to its higher thermal denat...
Tallennettuna:
| Julkaisussa: | Proc Natl Acad Sci U S A |
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| Päätekijät: | , , , |
| Aineistotyyppi: | Artigo |
| Kieli: | Inglês |
| Julkaistu: |
National Academy of Sciences
2003
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| Aiheet: | |
| Linkit: | https://ncbi.nlm.nih.govhttps://pmc.ncbi.nlm.nih.gov/articles/PMC208759/ https://ncbi.nlm.nih.govhttps://pubmed.ncbi.nlm.nih.gov/14504401/ https://ncbi.nlm.nih.govhttps://doi.org/10.1073/pnas.1635051100 |
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