ReviewAccounts of chemical research2024
Using 2D-IR Spectroscopy to Measure the Structure, Dynamics, and Intermolecular Interactions of Proteins in H
Review in Accounts of chemical research, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.
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Who cites it
21 citing papers in PubMed, 44 citations in OpenAlex.
- Multidimensional Infrared Spectroscopy as a Bioanalytical Technique.Chemical reviews · 2026Review
- Small extracellular vesicle-integrated by herbal hydrogels for spatiotemporal immunomodulation and neurovascular repair following traumatic brain injury.Bioactive materials · 2026Article
- AnFrontiers in chemistry · 2026Article
- Label-free linear and non-linear vibrational spectroscopy for functional materials: state-of-the-art and future perspectives.Chemical science · 2025Review
- Advances in Probing Amyloid Heterogeneity Using Vibrational Spectroscopy and Imaging.The journal of physical chemistry. B · 2025Review
- Fluorescence spectroscopy combined with molecular docking to study the interaction between folic acid derivatives from wheat grains and bovine trypsin.Scientific reports · 2025Article
- Exploring Water Beyond the Solvent: Insights into Density Fluctuations and EGFP Unfolding via Luminescence Thermometry.The journal of physical chemistry. B · 2025Article
- IR Spectroscopy: From Experimental Spectra to High-Resolution Structural Analysis by Integrating Simulations and Machine Learning.The journal of physical chemistry. B · 2025Article
- Multiscale theoretical study of infrared spectroscopy for the thermal denaturation process of aprotinin.Journal of molecular modeling · 2025Article
- Examining the Effect of an Anion-Binding Reagent on the Structure of Deprotonated Leucine Enkephalin Using Cryogenic-Ion Infrared Action Spectroscopy.The journal of physical chemistry. A · 2025Article
- Refining Structural Analysis of Proteins: Automated Methods to Measure Transition Dipole Strength of Single Residues.The journal of physical chemistry. B · 2025Article
- Two-dimensional bond-selective fluorescence spectroscopy: violations of the resonance condition, vibrational cooling rate dispersion, and super-multiplex imaging.Chemical science · 2025Article
- Unveiling Vibrational Couplings in Model Peptides in Solution by a Theoretical Approach.Molecules (Basel, Switzerland) · 2025Article
- Unlocking the Potential of Machine Learning in Enhancing Quantum Chemical Calculations for Infrared Spectral Prediction.ACS omega · 2025Article
- Emerging ultrafast technologies in biotechnology.3 Biotech · 2025Review
- Electric-Field Molecular Fingerprinting to Probe Cancer.ACS central science · 2025Article
- Role of Heavy Water in the Synthesis and Nanocatalytic Activity of Gold Nanoparticles.ACS nanoscience Au · 2025Article
- AI protocol for retrieving protein dynamic structures from two-dimensional infrared spectra.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Facile Generation of Cyanoselenocysteine as a Vibrational Label for Measuring Protein Dynamics on Longer Time Scales by 2D IR Spectroscopy.Analytical chemistry · 2025Article
- Fast Collective Hydrogen-Bond Dynamics in Hexafluoroisopropanol Related to its Chemical Activity.Angewandte Chemie (International ed. in English) · 2024Article
Corrections and comments
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Authors and funding
1 author at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Infrared (IR) spectroscopy probes molecular structure at the level of the chemical bond or functional group. In the case of proteins, the most informative band in the IR spectrum is the amide I band, which arises predominantly from the C═O stretching vibration of the peptide link. The folding of proteins into secondary and tertiary structures leads to vibrational coupling between peptide units, generating specific amide I spectral signatures that provide a fingerprint of the macromolecular conformation. Ultrafast two-dimensional IR (2D-IR) spectroscopy allows the amide I band of a protein to be spread over a second frequency dimension in a way that mirrors 2D-NMR methods. This means that amide I 2D-IR spectroscopy produces a spectral map that is exquisitely sensitive to protein structure and dynamics and so provides detailed insights that cannot be matched by IR absorption spectroscopy. As a result, 2D-IR spectroscopy has emerged as a powerful tool for probing protein structure and dynamics over a broad range of time and length scales in the solution phase at room temperature. However, the protein amide I band coincides with an IR absorption from the bending vibration of water (δ
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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.