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, alpha/beta protein L and the 66-residue, all-beta cold-shock protein Cs...

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Main Authors: Kusai A. Merchant, Robert B. Best, John M. Louis, Irina V. Gopich, William A. Eaton
格式: Artigo
語言:英语
出版: 2007
在線閱讀:https://doi.org/10.1073/pnas.0607097104
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