Quasi-analytical resolution-correction of elastic neutron scattering from proteins
Elastic neutron scattering from proteins reflects the motional amplitudes resulting from their internal collective and single-atom dynamics and is observable if the global diffusion of whole molecules is either blocked or cannot be resolved by the spectrometer under consideration. Due to finite inst...
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Veröffentlicht in: | The Journal of chemical physics 2022-10, Vol.157 (13), p.134103-134103 |
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creator | Hassani, Abir N. Stadler, Andreas M. Kneller, Gerald R. |
description | Elastic neutron scattering from proteins reflects the motional amplitudes resulting from their internal collective and single-atom dynamics and is observable if the global diffusion of whole molecules is either blocked or cannot be resolved by the spectrometer under consideration. Due to finite instrumental resolution, the measured elastic scattering amplitude always contains contaminations from quasielastic neutron scattering and some model must be assumed to extract the resolution-corrected counterpart from corresponding experimental spectra. Here, we derive a quasi-analytical method for that purpose, assuming that the intermediate scattering function relaxes with a “stretched” Mittag-Leffler function, Eα(−(t/τ)α) (0 < α < 1), toward the elastic amplitude and that the instrumental resolution function has Gaussian form. The corresponding function can be integrated into a fitting procedure and allows for eliminating the elastic intensity as a fit parameter. We illustrate the method for the analysis of two proteins in solution, the intrinsically disordered Myelin Basic Protein, confirming recently published results [Hassani et al., J. Chem. Phys. 156, 025102 (2022)], and the well-folded globular protein myoglobin. We also briefly discuss the consequences of our findings for the extraction of mean square position fluctuations from elastic scans. |
doi_str_mv | 10.1063/5.0103960 |
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Due to finite instrumental resolution, the measured elastic scattering amplitude always contains contaminations from quasielastic neutron scattering and some model must be assumed to extract the resolution-corrected counterpart from corresponding experimental spectra. Here, we derive a quasi-analytical method for that purpose, assuming that the intermediate scattering function relaxes with a “stretched” Mittag-Leffler function, Eα(−(t/τ)α) (0 < α < 1), toward the elastic amplitude and that the instrumental resolution function has Gaussian form. The corresponding function can be integrated into a fitting procedure and allows for eliminating the elastic intensity as a fit parameter. We illustrate the method for the analysis of two proteins in solution, the intrinsically disordered Myelin Basic Protein, confirming recently published results [Hassani et al., J. Chem. Phys. 156, 025102 (2022)], and the well-folded globular protein myoglobin. We also briefly discuss the consequences of our findings for the extraction of mean square position fluctuations from elastic scans.</description><identifier>ISSN: 0021-9606</identifier><identifier>EISSN: 1089-7690</identifier><identifier>DOI: 10.1063/5.0103960</identifier><identifier>CODEN: JCPSA6</identifier><language>eng</language><publisher>Melville: American Institute of Physics</publisher><subject>Chemical Physics ; Diffusion barriers ; Elastic scattering ; Myelin ; Myoglobins ; Neutron scattering ; Neutrons ; Physics ; Proteins ; Scattering amplitude ; Scattering functions</subject><ispartof>The Journal of chemical physics, 2022-10, Vol.157 (13), p.134103-134103</ispartof><rights>Author(s)</rights><rights>2022 Author(s). 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Due to finite instrumental resolution, the measured elastic scattering amplitude always contains contaminations from quasielastic neutron scattering and some model must be assumed to extract the resolution-corrected counterpart from corresponding experimental spectra. Here, we derive a quasi-analytical method for that purpose, assuming that the intermediate scattering function relaxes with a “stretched” Mittag-Leffler function, Eα(−(t/τ)α) (0 < α < 1), toward the elastic amplitude and that the instrumental resolution function has Gaussian form. The corresponding function can be integrated into a fitting procedure and allows for eliminating the elastic intensity as a fit parameter. We illustrate the method for the analysis of two proteins in solution, the intrinsically disordered Myelin Basic Protein, confirming recently published results [Hassani et al., J. Chem. Phys. 156, 025102 (2022)], and the well-folded globular protein myoglobin. We also briefly discuss the consequences of our findings for the extraction of mean square position fluctuations from elastic scans.</description><subject>Chemical Physics</subject><subject>Diffusion barriers</subject><subject>Elastic scattering</subject><subject>Myelin</subject><subject>Myoglobins</subject><subject>Neutron scattering</subject><subject>Neutrons</subject><subject>Physics</subject><subject>Proteins</subject><subject>Scattering amplitude</subject><subject>Scattering functions</subject><issn>0021-9606</issn><issn>1089-7690</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2022</creationdate><recordtype>article</recordtype><recordid>eNp90c9LBCEUB3CJgratQ__BQJcKpp4_xtHjslQbLERRZzFXy3DHUifov2-mjYIOnZQvn6eP9xA6xHCGgdPz5gwwUMlhC00wCFm3XMI2mgAQXA8x30V7Ob8AAG4Jm6C7215nX-tOh4_ijQ5VsjmGvvjY1SamZM14raKrbNB5IFVn-5KGKBtdik2-e6pciuvqNcVifZf30Y7TIduD73OKHi4v7ueLenlzdT2fLWtDhCz1qjHESYYNJY4JziTFQmvJ5UpICo7yR0F088gkoQ63rlmtQDLCTCuGAqcpnaKTzbvPOqjX5Nc6faiovVrMlmrMgGEhGG7e8WCPN3Zo8q23uai1z8aGoDsb-6xISyjmIPlIj_7Ql9inYT5fCrMGmrb9_dykmHOy7qcDDGrchGrU9yYGe7qx2fiix3H-gz8BFNaGvw</recordid><startdate>20221007</startdate><enddate>20221007</enddate><creator>Hassani, Abir N.</creator><creator>Stadler, Andreas M.</creator><creator>Kneller, Gerald R.</creator><general>American Institute of Physics</general><scope>AAYXX</scope><scope>CITATION</scope><scope>8FD</scope><scope>H8D</scope><scope>L7M</scope><scope>7X8</scope><scope>1XC</scope><orcidid>https://orcid.org/0000-0003-2272-5232</orcidid><orcidid>https://orcid.org/0000-0002-3374-3797</orcidid><orcidid>https://orcid.org/0000-0001-6906-9258</orcidid></search><sort><creationdate>20221007</creationdate><title>Quasi-analytical resolution-correction of elastic neutron scattering from proteins</title><author>Hassani, Abir N. ; Stadler, Andreas M. ; Kneller, Gerald R.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c289t-d5c2f941c32f48649318aa969d8930f36b82a5b4923f17f5dd09424c7832ffa33</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2022</creationdate><topic>Chemical Physics</topic><topic>Diffusion barriers</topic><topic>Elastic scattering</topic><topic>Myelin</topic><topic>Myoglobins</topic><topic>Neutron scattering</topic><topic>Neutrons</topic><topic>Physics</topic><topic>Proteins</topic><topic>Scattering amplitude</topic><topic>Scattering functions</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Hassani, Abir N.</creatorcontrib><creatorcontrib>Stadler, Andreas M.</creatorcontrib><creatorcontrib>Kneller, Gerald R.</creatorcontrib><collection>CrossRef</collection><collection>Technology Research Database</collection><collection>Aerospace Database</collection><collection>Advanced Technologies Database with Aerospace</collection><collection>MEDLINE - Academic</collection><collection>Hyper Article en Ligne (HAL)</collection><jtitle>The Journal of chemical physics</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Hassani, Abir N.</au><au>Stadler, Andreas M.</au><au>Kneller, Gerald R.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Quasi-analytical resolution-correction of elastic neutron scattering from proteins</atitle><jtitle>The Journal of chemical physics</jtitle><date>2022-10-07</date><risdate>2022</risdate><volume>157</volume><issue>13</issue><spage>134103</spage><epage>134103</epage><pages>134103-134103</pages><issn>0021-9606</issn><eissn>1089-7690</eissn><coden>JCPSA6</coden><abstract>Elastic neutron scattering from proteins reflects the motional amplitudes resulting from their internal collective and single-atom dynamics and is observable if the global diffusion of whole molecules is either blocked or cannot be resolved by the spectrometer under consideration. Due to finite instrumental resolution, the measured elastic scattering amplitude always contains contaminations from quasielastic neutron scattering and some model must be assumed to extract the resolution-corrected counterpart from corresponding experimental spectra. Here, we derive a quasi-analytical method for that purpose, assuming that the intermediate scattering function relaxes with a “stretched” Mittag-Leffler function, Eα(−(t/τ)α) (0 < α < 1), toward the elastic amplitude and that the instrumental resolution function has Gaussian form. The corresponding function can be integrated into a fitting procedure and allows for eliminating the elastic intensity as a fit parameter. We illustrate the method for the analysis of two proteins in solution, the intrinsically disordered Myelin Basic Protein, confirming recently published results [Hassani et al., J. Chem. Phys. 156, 025102 (2022)], and the well-folded globular protein myoglobin. 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subjects | Chemical Physics Diffusion barriers Elastic scattering Myelin Myoglobins Neutron scattering Neutrons Physics Proteins Scattering amplitude Scattering functions |
title | Quasi-analytical resolution-correction of elastic neutron scattering from proteins |
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