Open AccessNovel insights in linking solvent relaxation dynamics and protein conformations utilizing red edge excitation shift approach
Author(s) -
Rupasree Brahma,
H. Raghuraman
Publication year - 2021
Publication title -
emerging topics in life sciences
Language(s) - English
Resource type - Journals
eISSN - 2397-8562
pISSN - 2397-8554
DOI - 10.1042/etls20200256
Subject(s) - fluorophore , context (archaeology) , protein dynamics , solvation , dynamics (music) , relaxation (psychology) , chemical physics , stokes shift , excitation wavelength , chemistry , excitation , molecular dynamics , biophysics , fluorescence , nanotechnology , biological system , computational chemistry , materials science , physics , solvent , biology , biochemistry , neuroscience , paleontology , quantum mechanics , acoustics
Protein hydration dynamics plays an important role in many physiological processes since protein fluctuations, slow solvation, and the dynamics of hydrating water are all intrinsically related. Red edge excitation shift (REES) is a unique and powerful wavelength-selective (i.e. excitation-energy dependent) fluorescence approach that can be used to directly monitor the environment-induced restriction and dynamics around a polar fluorophore in a complex biological system. This review is mainly focused on recent applications of REES and a novel analysis of REES data to monitor the structural dynamics, functionally relevant conformational transitions and to unmask the structural ensembles in proteins. In addition, the novel utility of REES in imaging protein aggregates in a cellular context is discussed. We believe that the enormous potential of REES approach showcased in this review will engage more researchers, particularly from life sciences.