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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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Bibliografski detalji
Glavni autori: Bose, Kakoli, Clark, A. Clay
Format: Artigo
Jezik:Inglês
Izdano: Cold Spring Harbor Laboratory Press 2005
Teme:
Online pristup: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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