Measurement of protein non-covalent interactions in buffer and cells
Nuclear magnetic resonance (NMR) serves as a powerful tool for studying both the structure and dynamics of proteins. The NOE method, alongside residual dipolar; coupling, paramagnetic effects, J-coupling, and other related techniques, has reached a level of maturity that allows for the determination...
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KeAi Communications Co. Ltd.
2025-05-01
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| Series: | Magnetic Resonance Letters |
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| Online Access: | http://www.sciencedirect.com/science/article/pii/S2772516224000809 |
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| author | Jingwen Li Xiangfei Song Lishan Yao |
| author_facet | Jingwen Li Xiangfei Song Lishan Yao |
| author_sort | Jingwen Li |
| collection | DOAJ |
| description | Nuclear magnetic resonance (NMR) serves as a powerful tool for studying both the structure and dynamics of proteins. The NOE method, alongside residual dipolar; coupling, paramagnetic effects, J-coupling, and other related techniques, has reached a level of maturity that allows for the determination of protein structures. Furthermore, NMR relaxation methods prove to be highly effective in characterizing protein dynamics across various timescales. The properties of protein systems are dictated by intra- and intermolecular interactions among atoms, which involve covalent bonds, hydrogen bonds (H-bonds), electrostatic interactions, and van der Waals forces. Multiple NMR approaches have been developed to measure noncovalent interactions, and this paper offers a concise overview of noncovalent interaction measurements using NMR, with a specific emphasis on the advancements accomplished in our laboratory. |
| format | Article |
| id | doaj-art-e68e726401bc46039b74c477cd444cad |
| institution | Kabale University |
| issn | 2772-5162 |
| language | English |
| publishDate | 2025-05-01 |
| publisher | KeAi Communications Co. Ltd. |
| record_format | Article |
| series | Magnetic Resonance Letters |
| spelling | doaj-art-e68e726401bc46039b74c477cd444cad2025-08-20T03:26:20ZengKeAi Communications Co. Ltd.Magnetic Resonance Letters2772-51622025-05-015220017310.1016/j.mrl.2024.200173Measurement of protein non-covalent interactions in buffer and cellsJingwen Li0Xiangfei Song1Lishan Yao2College of Chemistry and Chemical Engineering, China University of Petroleum (East China), Qingdao, 266580, ChinaQingdao New Energy Shandong Laboratory, Qingdao Institute of Bioenergy and Bioprocess Technology, Chinese Academy of Sciences, Qingdao, 266101, China; Shandong Energy Institute, Qingdao, 266101, China; Corresponding author. Qingdao New Energy Shandong Laboratory, Qingdao Institute of Bioenergy and Bioprocess Technology, Chinese Academy of Sciences, Qingdao, 266101, China.Qingdao New Energy Shandong Laboratory, Qingdao Institute of Bioenergy and Bioprocess Technology, Chinese Academy of Sciences, Qingdao, 266101, China; Shandong Energy Institute, Qingdao, 266101, China; Corresponding author. Qingdao New Energy Shandong Laboratory, Qingdao Institute of Bioenergy and Bioprocess Technology, Chinese Academy of Sciences, Qingdao, 266101, China.Nuclear magnetic resonance (NMR) serves as a powerful tool for studying both the structure and dynamics of proteins. The NOE method, alongside residual dipolar; coupling, paramagnetic effects, J-coupling, and other related techniques, has reached a level of maturity that allows for the determination of protein structures. Furthermore, NMR relaxation methods prove to be highly effective in characterizing protein dynamics across various timescales. The properties of protein systems are dictated by intra- and intermolecular interactions among atoms, which involve covalent bonds, hydrogen bonds (H-bonds), electrostatic interactions, and van der Waals forces. Multiple NMR approaches have been developed to measure noncovalent interactions, and this paper offers a concise overview of noncovalent interaction measurements using NMR, with a specific emphasis on the advancements accomplished in our laboratory.http://www.sciencedirect.com/science/article/pii/S2772516224000809NMRH-bondCH/CH van der Waals interactionsQuinary interactionsElectrostatic interactionsCH/π and NH/π stacking interactions |
| spellingShingle | Jingwen Li Xiangfei Song Lishan Yao Measurement of protein non-covalent interactions in buffer and cells Magnetic Resonance Letters NMR H-bond CH/CH van der Waals interactions Quinary interactions Electrostatic interactions CH/π and NH/π stacking interactions |
| title | Measurement of protein non-covalent interactions in buffer and cells |
| title_full | Measurement of protein non-covalent interactions in buffer and cells |
| title_fullStr | Measurement of protein non-covalent interactions in buffer and cells |
| title_full_unstemmed | Measurement of protein non-covalent interactions in buffer and cells |
| title_short | Measurement of protein non-covalent interactions in buffer and cells |
| title_sort | measurement of protein non covalent interactions in buffer and cells |
| topic | NMR H-bond CH/CH van der Waals interactions Quinary interactions Electrostatic interactions CH/π and NH/π stacking interactions |
| url | http://www.sciencedirect.com/science/article/pii/S2772516224000809 |
| work_keys_str_mv | AT jingwenli measurementofproteinnoncovalentinteractionsinbufferandcells AT xiangfeisong measurementofproteinnoncovalentinteractionsinbufferandcells AT lishanyao measurementofproteinnoncovalentinteractionsinbufferandcells |