ArticleThe journal of physical chemistry. B2016
Infrared and Fluorescence Assessment of Protein Dynamics: From Folding to Function.
Article in The journal of physical chemistry. B, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed.
- A Fluorescence-Based Temperature-Jump Apparatus for Illustrating Protein Dynamics on the Millisecond Time Scale.Analytical chemistry · 2025Article
- Kinetic Mechanism of RNA Helix-Terminal Basepairing-A Kinetic Minima Network Analysis.Biophysical journal · 2019Article
- Exposing the Nucleation Site in α-Helix Folding: A Joint Experimental and Simulation Study.The journal of physical chemistry. B · 2019Article
- 4-Cyanoindole-2'-deoxyribonucleoside as a Dual Fluorescence and Infrared Probe of DNA Structure and Dynamics.Molecules (Basel, Switzerland) · 2019Article
- Ultrafast Hydrogen-Bonding Dynamics in Amyloid Fibrils.The journal of physical chemistry. B · 2018Article
- 7-Cyanoindole fluorescence as a local hydration reporter: application to probe the microheterogeneity of nine water-organic binary mixtures.Physical chemistry chemical physics : PCCP · 2018Article
- Possible Existence of α-Sheets in the Amyloid Fibrils Formed by a TTRJournal of the American Chemical Society · 2018Article
- Fermi resonance as a means to determine the hydrogen-bonding status of two infrared probes.Physical chemistry chemical physics : PCCP · 2017Article
- Activation pH and Gating Dynamics of Influenza A M2 Proton Channel Revealed by Single-Molecule Spectroscopy.Angewandte Chemie (International ed. in English) · 2017Article
- Simple method to introduce an ester infrared probe into proteins.Protein science : a publication of the Protein Society · 2017Article
- Infrared and fluorescence assessment of the hydration status of the tryptophan gate in the influenza A M2 proton channel.Physical chemistry chemical physics : PCCP · 2016Article
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Authors and funding
3 authors.
Funding
Abstract
While folding or performing functions, a protein can sample a rich set of conformational space. However, experimentally capturing all of the important motions with sufficient detail to allow a mechanistic description of their dynamics is nontrivial since such conformational events often occur over a wide range of time and length scales. Therefore, many methods have been employed to assess protein conformational dynamics, and depending on the nature of the conformational transition in question, some may be more advantageous than others. Herein, we describe our recent efforts, and also those of others, wherever appropriate, to use infrared- and fluorescence-based techniques to interrogate protein folding and functional dynamics. Specifically, we focus on discussing how to use extrinsic spectroscopic probes to enhance the structural resolution of these techniques and how to exploit various cross-linking strategies to acquire dynamic and mechanistic information that was previously difficult to attain.
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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.