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Changes in solvent exposure reveal the kinetics and equilibria of adsorbed protein unfolding in hydrophobic interaction chromatography
Hydrogen exchange has been a useful technique for studying the conformational state of proteins, both in bulk solution and at interfaces, for several decades. Here, we propose a physically-based model of simultaneous protein adsorption, unfolding and hydrogen exchange in HIC. An accompanying experim...
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| Hlavní autoři: | , , |
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| Médium: | Artigo |
| Jazyk: | Inglês |
| Vydáno: |
2010
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| Témata: | |
| On-line přístup: | https://ncbi.nlm.nih.gov/pmc/articles/PMC2956115/ https://ncbi.nlm.nih.gov/pubmed/20630532 https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1016/j.chroma.2010.06.051 |
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