Data Collection for Dilute Protein Solutions via a Neutron Backscattering Spectrometer
Understanding protein functions requires not only static but also dynamic structural information. Incoherent quasi-elastic neutron scattering (QENS), which utilizes the highly incoherent scattering ability of hydrogen, is a powerful technique for revealing the dynamics of proteins in deuterium oxide...
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MDPI AG
2022-05-01
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| author | Taiki Tominaga Hiroshi Nakagawa Masae Sahara Takashi Oda Rintaro Inoue Masaaki Sugiyama |
| author_facet | Taiki Tominaga Hiroshi Nakagawa Masae Sahara Takashi Oda Rintaro Inoue Masaaki Sugiyama |
| author_sort | Taiki Tominaga |
| collection | DOAJ |
| description | Understanding protein functions requires not only static but also dynamic structural information. Incoherent quasi-elastic neutron scattering (QENS), which utilizes the highly incoherent scattering ability of hydrogen, is a powerful technique for revealing the dynamics of proteins in deuterium oxide (D<sub>2</sub>O) buffer solutions. The background scattering of sample cells suitable for aqueous protein solution samples, conducted with a neutron backscattering spectrometer, was evaluated. It was found that the scattering intensity of an aluminum sample cell coated with boehmite using D<sub>2</sub>O was lower than that of a sample cell coated with regular water (H<sub>2</sub>O). The D<sub>2</sub>O-Boehmite coated cell was used for the QENS measurement of a 0.8 wt.% aqueous solution of an intrinsically disordered protein in an intrinsically disordered region of a helicase-associated endonuclease for a fork-structured type of DNA. The cell was inert against aqueous samples at 283–363 K. In addition, meticulous attention to cells with small individual weight differences and the positional reproducibility of the sample cell relative to the spectrometer neutron beam position enabled the accurate subtraction of the scattering profiles of the D<sub>2</sub>O buffer and the sample container. Consequently, high-quality information on protein dynamics could be extracted from dilute protein solutions. |
| first_indexed | 2024-03-10T03:33:29Z |
| format | Article |
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| institution | Directory Open Access Journal |
| issn | 2075-1729 |
| language | English |
| last_indexed | 2024-03-10T03:33:29Z |
| publishDate | 2022-05-01 |
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| spelling | doaj.art-2209564eae1f42a18823606da3a186172023-11-23T11:49:47ZengMDPI AGLife2075-17292022-05-0112567510.3390/life12050675Data Collection for Dilute Protein Solutions via a Neutron Backscattering SpectrometerTaiki Tominaga0Hiroshi Nakagawa1Masae Sahara2Takashi Oda3Rintaro Inoue4Masaaki Sugiyama5Neutron Science and Technology Center, Comprehensive Research Organization for Science and Society (CROSS), 162-1 Shirakata, Ibaraki 319-1106, JapanMaterials Sciences Research Center, Japan Atomic Energy Agency, Ibaraki 319-1195, JapanNeutron Science and Technology Center, Comprehensive Research Organization for Science and Society (CROSS), 162-1 Shirakata, Ibaraki 319-1106, JapanDepartment of Life Science, Rikkyo University, Nishi-Ikebukuro, Toshima-ku, Tokyo 171-8501, JapanInstitute for Integrated Radiation and Nuclear Science, Kyoto University, Kumatori, Sennan-gun, Osaka 590-0494, JapanInstitute for Integrated Radiation and Nuclear Science, Kyoto University, Kumatori, Sennan-gun, Osaka 590-0494, JapanUnderstanding protein functions requires not only static but also dynamic structural information. Incoherent quasi-elastic neutron scattering (QENS), which utilizes the highly incoherent scattering ability of hydrogen, is a powerful technique for revealing the dynamics of proteins in deuterium oxide (D<sub>2</sub>O) buffer solutions. The background scattering of sample cells suitable for aqueous protein solution samples, conducted with a neutron backscattering spectrometer, was evaluated. It was found that the scattering intensity of an aluminum sample cell coated with boehmite using D<sub>2</sub>O was lower than that of a sample cell coated with regular water (H<sub>2</sub>O). The D<sub>2</sub>O-Boehmite coated cell was used for the QENS measurement of a 0.8 wt.% aqueous solution of an intrinsically disordered protein in an intrinsically disordered region of a helicase-associated endonuclease for a fork-structured type of DNA. The cell was inert against aqueous samples at 283–363 K. In addition, meticulous attention to cells with small individual weight differences and the positional reproducibility of the sample cell relative to the spectrometer neutron beam position enabled the accurate subtraction of the scattering profiles of the D<sub>2</sub>O buffer and the sample container. Consequently, high-quality information on protein dynamics could be extracted from dilute protein solutions.https://www.mdpi.com/2075-1729/12/5/675protein solutiondynamicsQENSback scattering spectrometersample cellboehmite |
| spellingShingle | Taiki Tominaga Hiroshi Nakagawa Masae Sahara Takashi Oda Rintaro Inoue Masaaki Sugiyama Data Collection for Dilute Protein Solutions via a Neutron Backscattering Spectrometer Life protein solution dynamics QENS back scattering spectrometer sample cell boehmite |
| title | Data Collection for Dilute Protein Solutions via a Neutron Backscattering Spectrometer |
| title_full | Data Collection for Dilute Protein Solutions via a Neutron Backscattering Spectrometer |
| title_fullStr | Data Collection for Dilute Protein Solutions via a Neutron Backscattering Spectrometer |
| title_full_unstemmed | Data Collection for Dilute Protein Solutions via a Neutron Backscattering Spectrometer |
| title_short | Data Collection for Dilute Protein Solutions via a Neutron Backscattering Spectrometer |
| title_sort | data collection for dilute protein solutions via a neutron backscattering spectrometer |
| topic | protein solution dynamics QENS back scattering spectrometer sample cell boehmite |
| url | https://www.mdpi.com/2075-1729/12/5/675 |
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