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Charge–charge interactions in the denatured state influence the folding kinetics of ribonuclease Sa

Gaining a better understanding of the denatured state ensemble of proteins is important for understanding protein stability and the mechanism of protein folding. We studied the folding kinetics of ribonuclease Sa (RNase Sa) and a charge-reversal variant (D17R). The refolding kinetics are similar, bu...

詳細記述

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書誌詳細
主要な著者: Trefethen, Jared M., Pace, C. Nick, Scholtz, J. Martin, Brems, David N.
フォーマット: Artigo
言語:Inglês
出版事項: Cold Spring Harbor Laboratory Press 2005
主題:
オンライン・アクセス:https://ncbi.nlm.nih.gov/pmc/articles/PMC2253365/
https://ncbi.nlm.nih.gov/pubmed/15937282
https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1110/ps.051401905
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