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Watching Proteins in the Wild: Fluorescence Methods to Study Protein Dynamics in Living Cells
Author(s) -
Chamberlain Chester,
Hahn Klaus M.
Publication year - 2000
Publication title -
traffic
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 2.677
H-Index - 130
eISSN - 1600-0854
pISSN - 1398-9219
DOI - 10.1034/j.1600-0854.2000.011002.x
Subject(s) - protein dynamics , förster resonance energy transfer , biology , live cell imaging , green fluorescent protein , bimolecular fluorescence complementation , fluorescent protein , fluorescence , dynamics (music) , microbiology and biotechnology , living cell , biophysics , protein–protein interaction , computational biology , protein structure , cell , biochemistry , gene , physics , quantum mechanics , acoustics
The advent of GFP imaging has led to a revolution in the study of live cell protein dynamics. Ease of access to fluorescently tagged proteins has led to their widespread application and demonstrated the power of studying protein dynamics in living cells. This has spurred development of next generation approaches enabling not only the visualization of protein movements, but correlation of a protein's dynamics with its changing structural state or ligand binding. Such methods make use of fluorescence resonance energy transfer and dyes that report changes in their environment, and take advantage of new chemistries for site‐specific protein labeling.