ReviewEmerging topics in life sciences2021
Novel insights in linking solvent relaxation dynamics and protein conformations utilizing red edge excitation shift approach.
Review in Emerging topics in life sciences, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.
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Who cites it
15 citing papers in PubMed, 23 citations in OpenAlex.
- Anionic lipids modulate the membrane localization and conformational dynamics of KirBac1.1 slide helix during lipid-dependent activation.The Biochemical journal · 2025Article
- Self-Assembly Pathway Influence on Dehydropeptide-Based Gel Properties and Drug Release.Macromolecular bioscience · 2025Article
- HInternational journal of molecular sciences · 2025Review
- Structural Dynamics of the Slide Helix of Inactive/Closed Conformation of KirBac1.1 in Micelles and Membranes: A Fluorescence Approach.The Journal of membrane biology · 2025Article
- Characterization of a novel MgtE homolog and its structural dynamics in membrane mimetics.Biophysical journal · 2024Article
- Cholesterol modulates the structural dynamics of the paddle motif loop of KvAP voltage sensor.Current research in structural biology · 2024Article
- Red edge excitation shift spectroscopy is highly sensitive to tryptophan composition.Journal of the Royal Society, Interface · 2023Article
- Measuring Membrane Penetration Depths and Conformational Changes in Membrane Peptides and Proteins.The Journal of membrane biology · 2022Review
- Delving into Membrane Heterogeneity Utilizing Fluorescence Lifetime Distribution Analysis.The Journal of membrane biology · 2022Review
- Cost-effective Purification of Membrane Proteins using a Dual-detergent Strategy.Current protocols · 2022Article
- Site-directed fluorescence approaches to monitor the structural dynamics of proteins using intrinsic Trp and labeled with extrinsic fluorophores.STAR protocols · 2022Article
- Fluorescence Emission of Self-assembling Amyloid-like Peptides: Solution versus Solid State.Chemphyschem : a European journal of chemical physics and physical chemistry · 2021Article
- Lack of Environmental Sensitivity of a Naturally Occurring Fluorescent Analog of Cholesterol.Journal of fluorescence · 2021Article
- Environment-Sensitive Fluorescence of 7-Nitrobenz-2-oxa-1,3-diazol-4-yl (NBD)-Labeled Ligands for Serotonin Receptors.Molecules (Basel, Switzerland) · 2021Article
- A Thermodynamic Model for Interpreting Tryptophan Excitation-Energy-Dependent Fluorescence Spectra Provides Insight Into Protein Conformational Sampling and Stability.Frontiers in molecular biosciences · 2021Article
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
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.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.