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Unique fluorophores in the dimeric archaeal histones hMfB and hPyA1 reveal the impact of nonnative structure in a monomeric kinetic intermediate

Homodimeric archaeal histones and heterodimeric eukaryotic histones share a conserved structure but fold through different kinetic mechanisms, with a correlation between faster folding/association rates and the population of kinetic intermediates. Wild-type hMfB (from Methanothermus fervidus) has no...

詳細記述

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書誌詳細
主要な著者: Stump, Matthew R., Gloss, Lisa M.
フォーマット: Artigo
言語:Inglês
出版事項: Cold Spring Harbor Laboratory Press 2008
主題:
オンライン・アクセス:https://ncbi.nlm.nih.gov/pmc/articles/PMC2222717/
https://ncbi.nlm.nih.gov/pubmed/18096639
https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1110/ps.073224308
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