ArticleAccounts of chemical research2012
Three-dimensional structures by two-dimensional vibrational spectroscopy.
Article in Accounts of chemical research, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.
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Who cites it
27 citing papers in PubMed, 79 citations in OpenAlex.
- Multidimensional Infrared Spectroscopy as a Bioanalytical Technique.Chemical reviews · 2026Review
- Using 2D-IR Spectroscopy to Measure the Structure, Dynamics, and Intermolecular Interactions of Proteins in HAccounts of chemical research · 2024Review
- Biomolecular infrared spectroscopy: making time for dynamics.Chemical science · 2024Review
- Structural Dependence of Extended Amide III Vibrations in Two-Dimensional Infrared Spectra.The journal of physical chemistry letters · 2023Article
- Probing Ion Configurations in the KcsA Selectivity Filter with Single-Isotope Labels and 2D IR Spectroscopy.Journal of the American Chemical Society · 2023Article
- Inhibition of vibrational energy flow within an aromatic scaffold via heavy atom effect.The Journal of chemical physics · 2023Article
- The Role of Transmembrane Proteins in Plant Growth, Development, and Stress Responses.International journal of molecular sciences · 2022Review
- Applications of Single-Molecule Vibrational Spectroscopic Techniques for the Structural Investigation of Amyloid Oligomers.Molecules (Basel, Switzerland) · 2022Review
- Transparent window 2D IR spectroscopy of proteins.The Journal of chemical physics · 2021Review
- Protein Dynamics by Two-Dimensional Infrared Spectroscopy.Annual review of analytical chemistry (Palo Alto, Calif.) · 2021Article
- Tuning Molecular Vibrational Energy Flow within an Aromatic Scaffold via Anharmonic Coupling.The journal of physical chemistry. A · 2019Article
- Monolayer Sensitivity Enables a 2D IR Spectroscopic Immuno-biosensor for Studying Protein Structures: Application to Amyloid Polymorphs.The journal of physical chemistry letters · 2019Article
- Non-Additive Effects of Binding Site Mutations in Calmodulin.Biochemistry · 2019Article
- Site-Specific 1D and 2D IR Spectroscopy to Characterize the Conformations and Dynamics of Protein Molecular Recognition.The journal of physical chemistry. B · 2019Article
- RNA-Binding Protein RBP-P Is Required for Glutelin and Prolamine mRNA Localization in Rice Endosperm Cells.The Plant cell · 2018Article
- Coordination to lanthanide ions distorts binding site conformation in calmodulin.Proceedings of the National Academy of Sciences of the United States of America · 2018Article
- Watching Proteins Wiggle: Mapping Structures with Two-Dimensional Infrared Spectroscopy.Chemical reviews · 2017Review
- Refining Disordered Peptide Ensembles with Computational Amide I Spectroscopy: Application to Elastin-Like Peptides.The journal of physical chemistry. B · 2016Article
- Two-Dimensional Infrared Study of Vibrational Coupling between Azide and Nitrile Reporters in a RNA Nucleoside.The journal of physical chemistry. B · 2016Article
- Probing Site-Specific Structural Information of Peptides at Model Membrane Interface In Situ.Journal of the American Chemical Society · 2015Article
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
The development of experiments that can generate molecular movies of changing chemical structures is a major challenge for physical chemistry. But to realize this dream, we not only need to significantly improve existing approaches but also must invent new technologies. Most of the known protein structures have been determined by X-ray diffraction and to lesser extent by NMR. Though powerful, X-ray diffraction presents limitations for acquiring time-dependent structures. In the case of NMR, ultrafast equilibrium dynamics might be inferred from line shapes, but the structures of conformations interconverting on such time scales are not realizable. This Account highlights two-dimensional infrared spectroscopy (2D IR), in particular the 2D vibrational echo, as an approach to time-resolved structure determination. We outline the use of the 2D IR method to completely determine the structure of a protein of the integrin family in a time window of few picoseconds. As a transmembrane protein, this class of structures has proved particularly challenging for the established structural methodologies of X-ray crystallography and NMR. We describe the challenges facing multidimensional spectroscopy and compare it with some other methods of structural biology. Then we succinctly discuss the basic principles of 2D IR methods as they relate to time domain and frequency domain experimental and theoretical properties required for protein structure determination. By means of the example of the transmembrane protein, we describe the essential aspects of combined carbon-13-oxygen-18 isotope labels to create vibrational resonance pairs that allow the determination of protein and peptide structures in motion. Finally, we propose a three-dimensional structure of the αIIb transmembrane homodimer that includes optimum locations of all side chains and backbone atoms of the protein.
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