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Updated: May 14, 2026

Proton Transfer and Protein Conformation Dynamics in Photosensitive Proteins by Time-resolved Step-scan Fourier-transform Infrared Spectroscopy
Published on: June 27, 2014
Investigations of protein-protein interactions using time-resolved fluorescence and phasors
David M Jameson1, Carissa M Vetromile, Nicholas G James
1University 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
Abstract:
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.

