Ruggedness in the folding landscape of protein L

By exploring the folding pathways of the B1 domain of protein L with a series of equilibrium and rapid kinetic experiments, we have found its unfolded state to be more complex than suggested by two-state folding models. Using an ultrarapid mixer to initiate protein folding within ∼2–4 microseconds,...

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Detalhes bibliográficos
Main Authors: Waldauer, Steven A., Bakajin, Olgica, Ball, Terry, Chen, Yujie, DeCamp, Stephen J., Kopka, Michaela, Jäger, Marcus, Singh, Vijay R., Wedemeyer, William J., Weiss, Shimon, Yao, Shuhuai, Lapidus, Lisa J.
Formato: Artigo
Idioma:Inglês
Publicado em: HFSP Publishing 2008
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Articles
Acesso em linha:https://ncbi.nlm.nih.gov/pmc/articles/PMC2645578/
https://ncbi.nlm.nih.gov/pubmed/19436489
https://ncbi.nlm.nih.govhttp://dx.doi.org/10.2976/1.3013702
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