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- W2400106899 endingPage "5113" @default.
- W2400106899 startingPage "5103" @default.
- W2400106899 abstract "While folding or performing functions, a protein can sample a rich set of conformational space. However, experimentally capturing all of the important motions with sufficient detail to allow a mechanistic description of their dynamics is nontrivial since such conformational events often occur over a wide range of time and length scales. Therefore, many methods have been employed to assess protein conformational dynamics, and depending on the nature of the conformational transition in question, some may be more advantageous than others. Herein, we describe our recent efforts, and also those of others, wherever appropriate, to use infrared- and fluorescence-based techniques to interrogate protein folding and functional dynamics. Specifically, we focus on discussing how to use extrinsic spectroscopic probes to enhance the structural resolution of these techniques and how to exploit various cross-linking strategies to acquire dynamic and mechanistic information that was previously difficult to attain." @default.
- W2400106899 created "2016-06-24" @default.
- W2400106899 creator A5010160605 @default.
- W2400106899 creator A5015329154 @default.
- W2400106899 creator A5056319966 @default.
- W2400106899 date "2016-05-25" @default.
- W2400106899 modified "2023-10-11" @default.
- W2400106899 title "Infrared and Fluorescence Assessment of Protein Dynamics: From Folding to Function" @default.
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