PMID- 33416893
OWN - NLM
STAT- MEDLINE
DCOM- 20211022
LR  - 20220129
IS  - 2397-8554 (Print)
IS  - 2397-8562 (Electronic)
IS  - 2397-8554 (Linking)
VI  - 5
IP  - 1
DP  - 2021 May 14
TI  - Novel insights in linking solvent relaxation dynamics and protein conformations 
      utilizing red edge excitation shift approach.
PG  - 89-101
LID - 10.1042/ETLS20200256 [doi]
AB  - 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.
CI  - (c) 2021 The Author(s). Published by Portland Press Limited on behalf of the 
      Biochemical Society and the Royal Society of Biology.
FAU - Brahma, Rupasree
AU  - Brahma R
AD  - Crystallography and Molecular Biology Division, Saha Institute of Nuclear 
      Physics, Homi Bhabha National Institute, 1/AF Bidhannagar, Kolkata, India.
FAU - Raghuraman, H
AU  - Raghuraman H
AUID- ORCID: 0000-0001-9106-8278
AD  - Crystallography and Molecular Biology Division, Saha Institute of Nuclear 
      Physics, Homi Bhabha National Institute, 1/AF Bidhannagar, Kolkata, India.
LA  - eng
GR  - WT_/Wellcome Trust/United Kingdom
GR  - IA/I/17/2/503321/WTDBT_/DBT-Wellcome Trust India Alliance/India
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PT  - Review
PL  - England
TA  - Emerg Top Life Sci
JT  - Emerging topics in life sciences
JID - 101706399
RN  - 0 (Fluorescent Dyes)
RN  - 0 (Proteins)
RN  - 0 (Solvents)
SB  - IM
MH  - *Fluorescent Dyes
MH  - Protein Conformation
MH  - *Proteins
MH  - Solvents
MH  - Spectrometry, Fluorescence
PMC - PMC7611131
MID - EMS128608
OTO - NOTNLM
OT  - Trp and NBD fluorescence
OT  - conformational substates
OT  - hydration dynamics
OT  - protein matrix
OT  - red edge excitation shift (REES)
OT  - structural dynamics
COIS- Competing Interests The authors have no competing interests to declare.
EDAT- 2021/01/09 06:00
MHDA- 2021/11/18 06:00
PMCR- 2021/11/14
CRDT- 2021/01/08 12:13
PHST- 2020/10/21 00:00 [received]
PHST- 2020/12/14 00:00 [revised]
PHST- 2020/12/18 00:00 [accepted]
PHST- 2021/01/09 06:00 [pubmed]
PHST- 2021/11/18 06:00 [medline]
PHST- 2021/01/08 12:13 [entrez]
PHST- 2021/11/14 00:00 [pmc-release]
AID - 227540 [pii]
AID - 10.1042/ETLS20200256 [doi]
PST - ppublish
SO  - Emerg Top Life Sci. 2021 May 14;5(1):89-101. doi: 10.1042/ETLS20200256.