Characterizing the unfolded states of proteins using single-molecule FRET spectroscopy and molecular simulations

To obtain quantitative information on the size and dynamics of unfolded proteins we combined single-molecule lifetime and intensity FRET measurements with molecular simulations. We compared the unfolded states of the 64-residue, α/β protein L and the 66-residue, all-β cold-shock protein CspTm. The a...

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Autors principals: Merchant, Kusai A., Best, Robert B., Louis, John M., Gopich, Irina V., Eaton, William A.
Format: Artigo
Idioma:Inglês
Publicat: National Academy of Sciences 2007
Matèries:
Biological Sciences
Accés en línia:https://ncbi.nlm.nih.gov/pmc/articles/PMC1785253/
https://ncbi.nlm.nih.gov/pubmed/17251351
https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1073/pnas.0607097104
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