Electronic and Vibrational Second-Order Nonlinear Optical Properties of Protein Secondary Structural Motifs
A perturbation theory approach was developed for predicting the vibrational and electronic second-order nonlinear optical (NLO) polarizabilities of materials and macromolecules comprised of many coupled chromophores, with an emphasis on common protein secondary structural motifs. The polarization-de...
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| Veröffentlicht in: | The journal of physical chemistry. B 2005-10, Vol.109 (42), p.20009-20026 |
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| container_end_page | 20026 |
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| container_issue | 42 |
| container_start_page | 20009 |
| container_title | The journal of physical chemistry. B |
| container_volume | 109 |
| creator | Perry, John M Moad, Andrew J Begue, Nathan J Wampler, Ronald D Simpson, Garth J |
| description | A perturbation theory approach was developed for predicting the vibrational and electronic second-order nonlinear optical (NLO) polarizabilities of materials and macromolecules comprised of many coupled chromophores, with an emphasis on common protein secondary structural motifs. The polarization-dependent NLO properties of electronic and vibrational transitions in assemblies of amide chromophores comprising the polypeptide backbones of proteins were found to be accurately recovered in quantum chemical calculations by treating the coupling between adjacent oscillators perturbatively. A novel diagrammatic approach was developed to provide an intuitive visual means of interpreting the results of the perturbation theory calculations. Using this approach, the chiral and achiral polarization-dependent electronic SHG, isotropic SFG, and vibrational SFG nonlinear optical activities of protein structures were predicted and interpreted within the context of simple orientational models. |
| doi_str_mv | 10.1021/jp0506888 |
| format | Article |
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The polarization-dependent NLO properties of electronic and vibrational transitions in assemblies of amide chromophores comprising the polypeptide backbones of proteins were found to be accurately recovered in quantum chemical calculations by treating the coupling between adjacent oscillators perturbatively. A novel diagrammatic approach was developed to provide an intuitive visual means of interpreting the results of the perturbation theory calculations. 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Using this approach, the chiral and achiral polarization-dependent electronic SHG, isotropic SFG, and vibrational SFG nonlinear optical activities of protein structures were predicted and interpreted within the context of simple orientational models.</description><subject>Algorithms</subject><subject>Amino Acid Sequence</subject><subject>Electrons</subject><subject>Isomerism</subject><subject>Models, Chemical</subject><subject>Molecular Sequence Data</subject><subject>Nonlinear Dynamics</subject><subject>Protein Structure, Secondary</subject><subject>Proteins - chemistry</subject><issn>1520-6106</issn><issn>1520-5207</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2005</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNpt0MtOxCAUBmBiNN4XvoDpRhMXVaAt0KWZeIuXGZ3RLaH0NGHslAo00bcXM41uXBAg5-MAP0JHBJ8TTMnFsscFZkKIDbRLCorTOPjmuGYEsx205_0SY1pQwbbRDmGiyArBdtH7VQs6ONsZnaiuTt5M5VQwtlNtMgdtuzqduhpc8mS71nSgXDLtg9GxPHO2BxcM-MQ2P7sAphsPKfeVzIMbdBhcpI82mMYfoK1GtR4Ox3kfvV5fLSa36cP05m5y-ZCqnPCQqjIDUdVYkAJ0xTBrKCk1LbninFJWUMVyXDWKkzrngpW0ir8tG55lHAghIttHp-u-vbMfA_ggV8ZraFvVgR285JhwwnAe4dkaame9d9DI3plVfLskWP4kK3-TjfZ4bDpUK6j_5BhlBOkaGB_g87eu3LtkPOOFXMzmcvLyPMnf7p_kbfQna6-0l0s7uBi5_-fibxIfjpk</recordid><startdate>20051027</startdate><enddate>20051027</enddate><creator>Perry, John M</creator><creator>Moad, Andrew J</creator><creator>Begue, Nathan J</creator><creator>Wampler, Ronald D</creator><creator>Simpson, Garth J</creator><general>American Chemical Society</general><scope>BSCLL</scope><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>20051027</creationdate><title>Electronic and Vibrational Second-Order Nonlinear Optical Properties of Protein Secondary Structural Motifs</title><author>Perry, John M ; Moad, Andrew J ; Begue, Nathan J ; Wampler, Ronald D ; Simpson, Garth J</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-a417t-a93e8bd0815ecb606f219c297a7722652a640bfa71d478692b2079f7337e11183</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2005</creationdate><topic>Algorithms</topic><topic>Amino Acid Sequence</topic><topic>Electrons</topic><topic>Isomerism</topic><topic>Models, Chemical</topic><topic>Molecular Sequence Data</topic><topic>Nonlinear Dynamics</topic><topic>Protein Structure, Secondary</topic><topic>Proteins - chemistry</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Perry, John M</creatorcontrib><creatorcontrib>Moad, Andrew J</creatorcontrib><creatorcontrib>Begue, Nathan J</creatorcontrib><creatorcontrib>Wampler, Ronald D</creatorcontrib><creatorcontrib>Simpson, Garth J</creatorcontrib><collection>Istex</collection><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>The journal of physical chemistry. 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| identifier | ISSN: 1520-6106 |
| ispartof | The journal of physical chemistry. B, 2005-10, Vol.109 (42), p.20009-20026 |
| issn | 1520-6106 1520-5207 |
| language | eng |
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| source | MEDLINE; American Chemical Society Journals |
| subjects | Algorithms Amino Acid Sequence Electrons Isomerism Models, Chemical Molecular Sequence Data Nonlinear Dynamics Protein Structure, Secondary Proteins - chemistry |
| title | Electronic and Vibrational Second-Order Nonlinear Optical Properties of Protein Secondary Structural Motifs |
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