Insights into Protein Structure and Dynamics by Ultraviolet and Visible Resonance Raman Spectroscopy
| Autor: | Diana E. Schlamadinger, Brian S. Leigh, Ignacio López-Peña, Judy E. Kim |
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| Rok vydání: | 2015 |
| Předmět: |
inorganic chemicals
Quantitative Biology::Biomolecules Rhodopsin Chemistry Protein Conformation Resonance Raman spectroscopy technology industry and agriculture Resonance Infrared spectroscopy Inelastic scattering Chromophore Molecular Dynamics Simulation Photochemistry Spectrum Analysis Raman Biochemistry Article symbols.namesake symbols Animals Cattle Spectrophotometry Ultraviolet Coherent anti-Stokes Raman spectroscopy Raman spectroscopy Raman scattering |
| Zdroj: | Biochemistry. 54(31) |
| ISSN: | 1520-4995 |
| Popis: | 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. |
| Databáze: | OpenAIRE |
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