ArticleThe journal of physical chemistry letters2011
Elucidating Peptide and Protein Structure and Dynamics: UV Resonance Raman Spectroscopy.
Article in The journal of physical chemistry letters, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.
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Who cites it
19 citing papers in PubMed.
- Modeling Raman Spectra in Complex Environments: From Solutions to Surface-Enhanced Raman Scattering.The journal of physical chemistry letters · 2025Review
- Beyond the Visible: A Review of Ultraviolet Surface-Enhanced Raman Scattering Substrate Compositions, Morphologies, and Performance.Nanomaterials (Basel, Switzerland) · 2023Review
- UV-Resonance Raman Spectra of Systems in Complex Environments: A Multiscale Modeling Applied to Doxorubicin Intercalated into DNA.Journal of chemical information and modeling · 2023Article
- Amide Spectral Fingerprints are Hydrogen Bonding-Mediated.The journal of physical chemistry letters · 2022Article
- Insights Into the Mechanism of Tyrosine Nitration in Preventing β-Amyloid Aggregation in Alzheimer's Disease.Frontiers in molecular neuroscience · 2021Article
- pH-Dependent Conformational Changes of KcsA Tetramer and Monomer Probed by Raman Spectroscopy.International journal of molecular sciences · 2019Article
- Raman Sensing and Its Multimodal Combination with Optoacoustics and OCT for Applications in the Life Sciences.Sensors (Basel, Switzerland) · 2019Review
- Insights into Protein Structure and Dynamics by Ultraviolet and Visible Resonance Raman Spectroscopy.Biochemistry · 2015Article
- Unraveling the biomolecular snapshots of mitosis in healthy and cancer cells using plasmonically-enhanced Raman spectroscopy.Journal of the American Chemical Society · 2014Article
- Sodium dodecyl sulfate monomers induce XAO peptide polyproline II to α-helix transition.The journal of physical chemistry. B · 2014Article
- Temperature-sensitive gating of hCx26: high-resolution Raman spectroscopy sheds light on conformational changes.Biomedical optics express · 2014Article
- A robust and effective time-independent route to the calculation of Resonance Raman spectra of large molecules in condensed phases with the inclusion of Duschinsky, Herzberg-Teller, anharmonic, and environmental effects.Journal of chemical theory and computation · 2014Article
- Observation of persistent α-helical content and discrete types of backbone disorder during a molten globule to ordered peptide transition via deep-UV resonance Raman spectroscopy.Journal of Raman spectroscopy : JRS · 2013Article
- UV resonance Raman and DFT studies of arginine side chains in peptides: insights into arginine hydration.The journal of physical chemistry. B · 2013Article
- Two-Dimensional Stimulated Ultraviolet Resonance Raman Spectra of Tyrosine and Tryptophan; A Simulation Study.Journal of Raman spectroscopy : JRS · 2013Article
- Proton Coupled Electron Transfer and Redox Active Tyrosines: Structure and Function of the Tyrosyl Radicals in Ribonucleotide Reductase and Photosystem II.The journal of physical chemistry letters · 2012Article
- Spectroscopic studies of protein folding: linear and nonlinear methods.Protein science : a publication of the Protein Society · 2012Review
- β-hairpin forms by rolling up from C-terminal: topological guidance of early folding dynamics.Scientific reports · 2012Article
- Deep UV resonance Raman spectroscopy of β-sheet amyloid fibrils: a QM/MM simulation.The journal of physical chemistry. B · 2011Article
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Authors and funding
4 authors.
Funding
Abstract
UV resonance Raman spectroscopy (UVRR) is a powerful method that has the requisite selectivity and sensitivity to incisively monitor biomolecular structure and dynamics in solution. In this perspective, we highlight applications of UVRR for studying peptide and protein structure and the dynamics of protein and peptide folding. UVRR spectral monitors of protein secondary structure, such as the Amide III(3) band and the C(α)-H band frequencies and intensities can be used to determine Ramachandran Ψ angle distributions for peptide bonds. These incisive, quantitative glimpses into conformation can be combined with kinetic T-jump methodologies to monitor the dynamics of biomolecular conformational transitions. The resulting UVRR structural insight is impressive in that it allows differentiation of, for example, different α-helix-like states that enable differentiating π- and 3(10)- states from pure α-helices. These approaches can be used to determine the Gibbs free energy landscape of individual peptide bonds along the most important protein (un)folding coordinate. Future work will find spectral monitors that probe peptide bond activation barriers that control protein (un)folding mechanisms. In addition, UVRR studies of sidechain vibrations will probe the role of side chains in determining protein secondary, tertiary and quaternary structures.
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Registered trials
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