title: Infrared and Fluorescence Assessment of Protein Dynamics: From Folding to Function.
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.
authors.affiliation: Department of Chemistry and ‡The Ultrafast Optical Processes Laboratory, University of Pennsylvania , Philadelphia, Pennsylvania 19104, United States.
authors.forename: Bei
authors.initials: B
authors.lastname: Ding
authors.affiliation: Department of Chemistry and ‡The Ultrafast Optical Processes Laboratory, University of Pennsylvania , Philadelphia, Pennsylvania 19104, United States.
authors.forename: Mary Rose
authors.initials: MR
authors.lastname: Hilaire
authors.affiliation: Department of Chemistry and ‡The Ultrafast Optical Processes Laboratory, University of Pennsylvania , Philadelphia, Pennsylvania 19104, United States.
authors.forename: Feng
authors.initials: F
authors.lastname: Gai
mesh_terms: D031541:Fluorescence Resonance Energy Transfer; D007700:Kinetics; D017510:Protein Folding; D011506:Proteins / Q000737:chemistry*; D013055:Spectrophotometry, Infrared
chemical_list: D011506:Proteins