Vibrational spectra of room-temperature rhodopsin: concentration dependence in picosecond resonance coherent anti-Stokes Raman scattering
The vibrational degrees of freedom of room-temperature rhodopsin (Rh RT), the central trans-membrane protein in vision, are measured at room temperature by picosecond resonance coherent anti-Stokes Raman scattering (PR/CARS). High signal-to-noise PR/CARS data for the ethylenic stretching, Schiff bas...
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| Veröffentlicht in: | Biophysical chemistry 1995-09, Vol.56 (1), p.129-135 |
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| creator | Popp, A. Ujj, L. Atkinson, G.H. |
| description | The vibrational degrees of freedom of room-temperature rhodopsin (Rh
RT), the central trans-membrane protein in vision, are measured at room temperature by picosecond resonance coherent anti-Stokes Raman scattering (PR/CARS). High signal-to-noise PR/CARS data for the ethylenic stretching, Schiff base, and hydrogen-out-of-plane modes of the retinal chromophore are quantitatively analyzed via third-order susceptibility relationships. The accurate determination of spectral features permit the PR/CARS bandshapes to be analyzed as a function of Rh
RT concentration, an essential factor in using picosecond time-resolved CARS techniques to measure the vibrational spectroscopy of picosecond intermediates in the Rh
RT photosequence. Of particular importance is the recognition that PR/CARS bandshapes are sensitive functions of both the chromophore concentration and the excitation wavelength, as measured relative to the absorption spectra of specific chromophores (static and transient). |
| doi_str_mv | 10.1016/0301-4622(95)00024-R |
| format | Article |
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RT), the central trans-membrane protein in vision, are measured at room temperature by picosecond resonance coherent anti-Stokes Raman scattering (PR/CARS). High signal-to-noise PR/CARS data for the ethylenic stretching, Schiff base, and hydrogen-out-of-plane modes of the retinal chromophore are quantitatively analyzed via third-order susceptibility relationships. The accurate determination of spectral features permit the PR/CARS bandshapes to be analyzed as a function of Rh
RT concentration, an essential factor in using picosecond time-resolved CARS techniques to measure the vibrational spectroscopy of picosecond intermediates in the Rh
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RT), the central trans-membrane protein in vision, are measured at room temperature by picosecond resonance coherent anti-Stokes Raman scattering (PR/CARS). High signal-to-noise PR/CARS data for the ethylenic stretching, Schiff base, and hydrogen-out-of-plane modes of the retinal chromophore are quantitatively analyzed via third-order susceptibility relationships. The accurate determination of spectral features permit the PR/CARS bandshapes to be analyzed as a function of Rh
RT concentration, an essential factor in using picosecond time-resolved CARS techniques to measure the vibrational spectroscopy of picosecond intermediates in the Rh
RT photosequence. Of particular importance is the recognition that PR/CARS bandshapes are sensitive functions of both the chromophore concentration and the excitation wavelength, as measured relative to the absorption spectra of specific chromophores (static and transient).</description><subject>Animals</subject><subject>Cattle</subject><subject>Coherent spectroscopy</subject><subject>Kinetics</subject><subject>Picosecond spectroscopy</subject><subject>Protein Conformation</subject><subject>Raman</subject><subject>Retinaldehyde - metabolism</subject><subject>Rhodopsin</subject><subject>Rhodopsin - chemistry</subject><subject>Rhodopsin - metabolism</subject><subject>Scattering, Radiation</subject><subject>Spectrum Analysis, Raman - methods</subject><subject>Temperature</subject><subject>Time Factors</subject><subject>Vision</subject><issn>0301-4622</issn><issn>1873-4200</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1995</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNp9kUtrFTEUx4NY6rX6DRSyErsYm2QyScZFQYovKBSuj23I44yN3kmmSa7Qj-C3NuO9dOkqcP6PcH4HoReUvKGEigvSE9pxwdjrcTgnhDDebR-hDVWy7zgj5DHaPFieoKel_Gwmogg5RadSCKYE3aA_34PNpoYUzQ6XBVzNBqcJ55TmrsK8QFP3GXC-TT4tJcS32KXoINZDDHtYIHpoIxwiXoJLBZrD4wylta5zl24htwQ2sYbuS02_oOCtmU3ExZlaIYf44xk6mcyuwPPje4a-fXj_9epTd33z8fPVu-vO9YOsnTDECjmCGqeBqIE468SghFS8t6N1ivSTp9RQJi1TI7fWTpwzL_zkqGrZ_gy9OvQuOd3toVQ9h-JgtzMR0r5oKflI5ciakR-MLqdSMkx6yWE2-V5TotcL6BWvXvHqcdD_LqC3Lfby2L-3M_iH0BF50y8POrQlfwfIuriw4vMhN_zap_D_D_4CM9eY9w</recordid><startdate>19950901</startdate><enddate>19950901</enddate><creator>Popp, A.</creator><creator>Ujj, L.</creator><creator>Atkinson, G.H.</creator><general>Elsevier B.V</general><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7X8</scope></search><sort><creationdate>19950901</creationdate><title>Vibrational spectra of room-temperature rhodopsin: concentration dependence in picosecond resonance coherent anti-Stokes Raman scattering</title><author>Popp, A. ; Ujj, L. ; Atkinson, G.H.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c357t-6a0b679e89f50850cbc65867843b9bc803fd11a127b2894bbbf442d6dfc18a0b3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1995</creationdate><topic>Animals</topic><topic>Cattle</topic><topic>Coherent spectroscopy</topic><topic>Kinetics</topic><topic>Picosecond spectroscopy</topic><topic>Protein Conformation</topic><topic>Raman</topic><topic>Retinaldehyde - metabolism</topic><topic>Rhodopsin</topic><topic>Rhodopsin - chemistry</topic><topic>Rhodopsin - metabolism</topic><topic>Scattering, Radiation</topic><topic>Spectrum Analysis, Raman - methods</topic><topic>Temperature</topic><topic>Time Factors</topic><topic>Vision</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Popp, A.</creatorcontrib><creatorcontrib>Ujj, L.</creatorcontrib><creatorcontrib>Atkinson, G.H.</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>MEDLINE - Academic</collection><jtitle>Biophysical chemistry</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Popp, A.</au><au>Ujj, L.</au><au>Atkinson, G.H.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Vibrational spectra of room-temperature rhodopsin: concentration dependence in picosecond resonance coherent anti-Stokes Raman scattering</atitle><jtitle>Biophysical chemistry</jtitle><addtitle>Biophys Chem</addtitle><date>1995-09-01</date><risdate>1995</risdate><volume>56</volume><issue>1</issue><spage>129</spage><epage>135</epage><pages>129-135</pages><issn>0301-4622</issn><eissn>1873-4200</eissn><abstract>The vibrational degrees of freedom of room-temperature rhodopsin (Rh
RT), the central trans-membrane protein in vision, are measured at room temperature by picosecond resonance coherent anti-Stokes Raman scattering (PR/CARS). High signal-to-noise PR/CARS data for the ethylenic stretching, Schiff base, and hydrogen-out-of-plane modes of the retinal chromophore are quantitatively analyzed via third-order susceptibility relationships. The accurate determination of spectral features permit the PR/CARS bandshapes to be analyzed as a function of Rh
RT concentration, an essential factor in using picosecond time-resolved CARS techniques to measure the vibrational spectroscopy of picosecond intermediates in the Rh
RT photosequence. Of particular importance is the recognition that PR/CARS bandshapes are sensitive functions of both the chromophore concentration and the excitation wavelength, as measured relative to the absorption spectra of specific chromophores (static and transient).</abstract><cop>Netherlands</cop><pub>Elsevier B.V</pub><pmid>7662861</pmid><doi>10.1016/0301-4622(95)00024-R</doi><tpages>7</tpages></addata></record> |
| fulltext | fulltext |
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| ispartof | Biophysical chemistry, 1995-09, Vol.56 (1), p.129-135 |
| issn | 0301-4622 1873-4200 |
| language | eng |
| recordid | cdi_proquest_miscellaneous_77491792 |
| source | MEDLINE; Elsevier ScienceDirect Journals Complete |
| subjects | Animals Cattle Coherent spectroscopy Kinetics Picosecond spectroscopy Protein Conformation Raman Retinaldehyde - metabolism Rhodopsin Rhodopsin - chemistry Rhodopsin - metabolism Scattering, Radiation Spectrum Analysis, Raman - methods Temperature Time Factors Vision |
| title | Vibrational spectra of room-temperature rhodopsin: concentration dependence in picosecond resonance coherent anti-Stokes Raman scattering |
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