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10.1021/acs.biochem.5b00514

http://scihub22266oqcxt.onion/10.1021/acs.biochem.5b00514
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C5092233!5092233!26219819
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suck abstract from ncbi


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pmid26219819      Biochemistry 2015 ; 54 (31): 4770-83
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  • Insights into Protein Structure and Dynamics by Ultraviolet and Visible Resonance Raman Spectroscopy #MMPMID26219819
  • López-Peña I; Leigh BS; Schlamadinger DE; Kim JE
  • Biochemistry 2015[Aug]; 54 (31): 4770-83 PMID26219819show ga
  • 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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