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10.1021/acs.biochem.5b00514 http://scihub22266oqcxt.onion/10.1021/acs.biochem.5b00514 C5092233!5092233 !26219819     free     free     free Deprecated: Implicit conversion from float 211.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 211.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 211.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 211.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 211.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 211.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 245.2 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 245.2 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Warning: imagejpeg(C:\Inetpub\vhosts\kidney.de\httpdocs\phplern\26219819 .jpg): Failed to open stream: No such file or directory in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 117       Biochemistry 2015 ; 54 (31 ): 4770-83 Nephropedia Template TP {{tp|p=26219819 |t=2015. Insights into Protein Structure and Dynamics by Ultraviolet and Visible Resonance Raman Spectroscopy |pdf=|usr=}}{{26219819 }} gab.com Text Insights into Protein Structure and Dynamics by Ultraviolet and Visible Resonance Raman Spectroscopy JO: Biochemistry http://www.kidney.de/pget.php?&tw=1&pmid=26219819 #FOAvip 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. Twit Text FOAVip Insights into Protein Structure and Dynamics by Ultraviolet and Visible Resonance Raman Spectroscopy ????Biochemistry http://www.kidney.de/pget.php?&tw=1&pmid=26219819 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=26219819 #FOAvip English Wikipedia <ref>{{Cite pmid|26219819 }}</ref> 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 PMID26219819 show 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. |*Molecular Dynamics Simulation [MESH] |Animals [MESH] |Cattle [MESH] |Protein Conformation [MESH] |Rhodopsin/*chemistry [MESH] |Spectrophotometry, Ultraviolet/methods [MESH]Insights into Protein Structure and Dynamics by Ultraviolet and Visibl(epmc).pdf DeepDyve Pubget Overpricing