Investigations of protein-protein interactions using time-resolved fluorescence and phasors.
Protein interactions are critical for biological specificity and techniques able to characterize these interactions are of fundamental importance in biochemistry and cell biology. Fluorescence methodologies have been extremely useful for studying many biological systems including protein-ligand and protein-protein interactions. In this review we focus on the application of time-resolved fluorescence approaches to macromolecular systems. We also include a detailed discussion of a relatively new time-resolved technique, the phasor method, for studying protein interactions both in vitro and in live cells.
University of Hawaii, Department of Cell and Molecular Biology, John A. Burns School of Medicine, 651 Ilalo St., BSB222, Honolulu, HI 96813, USA. djameson@hawaii.edu
David M
DM
Jameson
Carissa M
CM
Vetromile
Nicholas G
NG
James
D005454:Fluorescence Polarization; D031541:Fluorescence Resonance Energy Transfer / Q000379:methods; D007091:Image Processing, Computer-Assisted; D008856:Microscopy, Fluorescence / Q000379:methods*; D025941:Protein Interaction Mapping / Q000379:methods*; D011506:Proteins / Q000378:metabolism*; D012984:Software; D013997:Time Factors
D011506:Proteins