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Identification of Residual Structure in the Unfolded State of Ribonuclease H1 from the Moderately Thermophilic Chlorobium tepidum: Comparison with Thermophilic and Mesophilic Homologues
Ribonucleases H from organisms that grow at different temperatures demonstrate a variable change in heat capacity upon unfolding (ΔC°(P)) [Ratcliff, K., et al. (2009) Biochemistry 48, 5890–5898]. This ΔC°(P) has been shown to correlate with a tolerance to higher temperatures and residual structure i...
Bewaard in:
| Hoofdauteurs: | , |
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| Formaat: | Artigo |
| Taal: | Inglês |
| Gepubliceerd in: |
2010
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| Onderwerpen: | |
| Online toegang: | https://ncbi.nlm.nih.gov/pmc/articles/PMC2903448/ https://ncbi.nlm.nih.gov/pubmed/20491485 https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1021/bi1001097 |
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