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Increasing the Net Charge and Decreasing the Hydrophobicity of Bovine Carbonic Anhydrase Decreases the Rate of Denaturation with Sodium Dodecyl Sulfate

This study compares the rate of denaturation with sodium dodecyl sulfate (SDS) of the individual rungs of protein charge ladders generated by acylation of the lysine [Formula: see text] groups of bovine carbonic anhydrase II (BCA). Each acylation decreases the number of positively charged groups, in...

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Autori principali: Gudiksen, Katherine L., Gitlin, Irina, Moustakas, Demetri T., Whitesides, George M.
Natura: Artigo
Lingua:Inglês
Pubblicazione: Biophysical Society 2006
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Accesso online:https://ncbi.nlm.nih.gov/pmc/articles/PMC1479075/
https://ncbi.nlm.nih.gov/pubmed/16617087
https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1529/biophysj.106.081547
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