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Understanding the Thermal Denaturation of Myoglobin with IMS-MS: Evidence for Multiple Stable Structures and Trapped Pre-equilibrium States
Thermal denaturation of holomyoglobin (hMb) in solution (10 mM ammonium acetate at pH = 4.5, 6.8, and 9.0) was monitored by ion mobility spectrometry (IMS) and mass spectrometry (MS) techniques to characterize the stability and investigate structural changes involved in unfolding. We utilize two exp...
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| Опубликовано в: : | J Am Soc Mass Spectrom |
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| Главные авторы: | , , , , |
| Формат: | Artigo |
| Язык: | Inglês |
| Опубликовано: |
2020
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| Предметы: | |
| Online-ссылка: | https://ncbi.nlm.nih.gov/pmc/articles/PMC7790998/ https://ncbi.nlm.nih.gov/pubmed/32539412 https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1021/jasms.0c00075 |
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