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Experimental evaluation of topological parameters determining protein-folding rates

Recent work suggests that structural topology plays a key role in determining protein-folding rates and pathways. The refolding rates of small proteins that fold without intermediates are found to correlate with simple structural parameters such as relative contact order, long-range order, or the fr...

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書誌詳細
出版年:Proc Natl Acad Sci U S A
主要な著者: Miller, Erik J., Fischer, Kael F., Marqusee, Susan
フォーマット: Artigo
言語:Inglês
出版事項: National Academy of Sciences 2002
主題:
オンライン・アクセス:https://ncbi.nlm.nih.govhttps://pmc.ncbi.nlm.nih.gov/articles/PMC124919/
https://ncbi.nlm.nih.govhttps://pubmed.ncbi.nlm.nih.gov/12149462/
https://ncbi.nlm.nih.govhttps://doi.org/10.1073/pnas.162219099
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