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Temperature dependence of protein motions in a thermophilic dihydrofolate reductase and its relationship to catalytic efficiency
We report hydrogen deuterium exchange by mass spectrometry (HDX-MS) as a function of temperature in a thermophilic dihydrofolate reductase from Bacillus stearothermophilus (Bs-DHFR). Protein stability, probed with circular dichroism, established an accessible temperature range of 10 °C to 55 °C for...
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| Main Authors: | , , , , , |
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| Format: | Artigo |
| Sprog: | Inglês |
| Udgivet: |
National Academy of Sciences
2010
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| Fag: | |
| Online adgang: | https://ncbi.nlm.nih.gov/pmc/articles/PMC2890430/ https://ncbi.nlm.nih.gov/pubmed/20534574 https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1073/pnas.1003678107 |
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