ArticleBiochemistry2015
Insights into Protein Structure and Dynamics by Ultraviolet and Visible Resonance Raman Spectroscopy.
Article in Biochemistry, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
9 citing papers in PubMed.
- Online Raman spectroscopy-guided strategy for efficient production of DNA recombinase UvsX in Escherichia coli.Analytical and bioanalytical chemistry · 2026Article
- Early Sepsis Diagnosis as a Global Imperative: The Role of Raman Spectroscopy.Journal of clinical medicine · 2026Review
- Does Transglutaminase Crosslinking Reduce the Antibody Recognition Capacity of β-Lactoglobulin: An Analysis from Conformational Perspective.Molecules (Basel, Switzerland) · 2025Article
- Lighting the Path: Raman Spectroscopy's Journey Through the Microbial Maze.Molecules (Basel, Switzerland) · 2024Article
- Selective excitation of vibrations in a single molecule.Nature communications · 2024Article
- The degree of doneness affected molecular changes and protein digestibility of pork.Frontiers in nutrition · 2022Article
- UV Resonance Raman explores protein structural modification upon fibrillation and ligand interaction.Biophysical journal · 2021Article
- A critical review of recent trends, and a future perspective of optical spectroscopy as PAT in biopharmaceutical downstream processing.Analytical and bioanalytical chemistry · 2020Review
- UV Resonance Raman Spectroscopy as a Tool to Probe Membrane Protein Structure and Dynamics.Methods in molecular biology (Clifton, N.J.) · 2019Article
Corrections and comments
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Authors and funding
4 authors.
Funding
Abstract
Raman spectroscopy is a form of vibrational spectroscopy based on inelastic scattering of light. In resonance Raman spectroscopy, the wavelength of the incident light falls within an absorption band of a chromophore, and this overlap of excitation and absorption energy greatly enhances the Raman scattering efficiency of the absorbing species. The ability to probe vibrational spectra of select chromophores within a complex mixture of molecules makes resonance Raman spectroscopy an excellent tool for studies of biomolecules. In this Current Topic, we discuss the type of molecular insights obtained from steady-state and time-resolved resonance Raman studies of a prototypical photoactive protein, rhodopsin. We also review recent efforts in ultraviolet resonance Raman investigations of soluble and membrane-associated biomolecules, including integral membrane proteins and antimicrobial peptides. These examples illustrate that resonance Raman is a sensitive, selective, and practical method for studying the structures of biological molecules, and the molecular bonding, geometry, and environments of protein cofactors, the backbone, and side chains.
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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.