Conformational Change in Unsolvated Trp-cage Protein Probed by Fluorescence

摘要

Characterization of the structure and dynamics of biopolymers is of paramount importance to understanding life processes at the molecular level.Measurements of these molecules in the absence of a solvent or surface are useful for elucidating the effects of the solvent environment on the native structure and dynamics.Mass spectrometry-based measurements of ion mobility and ion-molecule and dissociation reactions have been used to detect global conformational change in unsolvated biopolymers.We have been applying fluorescence spectroscopy to unsolvated biomolecule ions to take advantage of the unique ability of this technique to directly probe the local molecular environment surrounding the fluorophore.