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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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Detalhes bibliográficos
Main Authors: Oyeyemi, Olayinka A., Sours, Kevin M., Lee, Thomas, Resing, Katheryn A., Ahn, Natalie G., Klinman, Judith P.
Formato: Artigo
Idioma:Inglês
Publicado em: National Academy of Sciences 2010
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Acesso em linha: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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