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Unfolded DapA forms aggregates when diluted into free solution, confounding comparison with folding by the GroEL/GroES chaperonin system

A recent hydrogen-deuterium exchange study of folding of the GroEL/GroES-dependent bacterial enzyme DapA has suggested that the DapA folding pathway when free in solution may differ from the folding pathway used in the presence of the GroEL/GroES chaperonin. Here, we have investigated whether DapA a...

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書目詳細資料
發表在:FEBS Lett
Main Authors: Ambrose, Andrew, Fenton, Wayne, Mason, Damian J., Chapman, Eli, Horwich, Arthur L.
格式: Artigo
語言:Inglês
出版: 2015
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在線閱讀:https://ncbi.nlm.nih.gov/pmc/articles/PMC4410871/
https://ncbi.nlm.nih.gov/pubmed/25601566
https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1016/j.febslet.2015.01.008
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