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pH effects on the stability and dimerization of procaspase-3
pH-dependent conformational changes are known to occur in dimeric procaspase-3, and they have been shown to affect the rate of automaturation. We studied the equilibrium unfolding of procaspase-3(C163S) as a function of pH (between pH 8.5 and pH 4) in order to examine these changes in the context of...
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| Hauptverfasser: | , |
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| Format: | Artigo |
| Sprache: | Inglês |
| Veröffentlicht: |
Cold Spring Harbor Laboratory Press
2005
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| Schlagworte: | |
| Online Zugang: | https://ncbi.nlm.nih.gov/pmc/articles/PMC2253328/ https://ncbi.nlm.nih.gov/pubmed/15576551 https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1110/ps.041003305 |
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