[{"ddc":["570"],"volume":82,"acknowledgement":"We thank Petra Rovó for critical reading of this manuscript. We acknowledge the Austrian Science Foundation FWF (project AlloSpace, number I5812–B) and funding by the Institute of Science and Technology Austria.","isi":1,"external_id":{"isi":["001053616200001"],"pmid":["37536064"]},"date_updated":"2024-01-30T12:37:36Z","year":"2023","citation":{"ista":"Napoli F, Becker LM, Schanda P. 2023. Protein dynamics detected by magic-angle spinning relaxation dispersion NMR. Current Opinion in Structural Biology. 82(10), 102660.","mla":"Napoli, Federico, et al. “Protein Dynamics Detected by Magic-Angle Spinning Relaxation Dispersion NMR.” <i>Current Opinion in Structural Biology</i>, vol. 82, no. 10, 102660, Elsevier, 2023, doi:<a href=\"https://doi.org/10.1016/j.sbi.2023.102660\">10.1016/j.sbi.2023.102660</a>.","short":"F. Napoli, L.M. Becker, P. Schanda, Current Opinion in Structural Biology 82 (2023).","ieee":"F. Napoli, L. M. Becker, and P. Schanda, “Protein dynamics detected by magic-angle spinning relaxation dispersion NMR,” <i>Current Opinion in Structural Biology</i>, vol. 82, no. 10. Elsevier, 2023.","chicago":"Napoli, Federico, Lea Marie Becker, and Paul Schanda. “Protein Dynamics Detected by Magic-Angle Spinning Relaxation Dispersion NMR.” <i>Current Opinion in Structural Biology</i>. Elsevier, 2023. <a href=\"https://doi.org/10.1016/j.sbi.2023.102660\">https://doi.org/10.1016/j.sbi.2023.102660</a>.","apa":"Napoli, F., Becker, L. M., &#38; Schanda, P. (2023). Protein dynamics detected by magic-angle spinning relaxation dispersion NMR. <i>Current Opinion in Structural Biology</i>. Elsevier. <a href=\"https://doi.org/10.1016/j.sbi.2023.102660\">https://doi.org/10.1016/j.sbi.2023.102660</a>","ama":"Napoli F, Becker LM, Schanda P. Protein dynamics detected by magic-angle spinning relaxation dispersion NMR. <i>Current Opinion in Structural Biology</i>. 2023;82(10). doi:<a href=\"https://doi.org/10.1016/j.sbi.2023.102660\">10.1016/j.sbi.2023.102660</a>"},"abstract":[{"text":"Magic-angle spinning (MAS) nuclear magnetic resonance (NMR) is establishing itself as a powerful method for the characterization of protein dynamics at the atomic scale. We discuss here how R1ρ MAS relaxation dispersion NMR can explore microsecond-to-millisecond motions. Progress in instrumentation, isotope labeling, and pulse sequence design has paved the way for quantitative analyses of even rare structural fluctuations. In addition to isotropic chemical-shift fluctuations exploited in solution-state NMR relaxation dispersion experiments, MAS NMR has a wider arsenal of observables, allowing to see motions even if the exchanging states do not differ in their chemical shifts. We demonstrate the potential of the technique for probing motions in challenging large enzymes, membrane proteins, and protein assemblies.","lang":"eng"}],"doi":"10.1016/j.sbi.2023.102660","day":"01","file_date_updated":"2024-01-30T12:36:39Z","quality_controlled":"1","article_type":"original","publisher":"Elsevier","author":[{"id":"d42e08e7-f4fc-11eb-af0a-d71e26138f1b","first_name":"Federico","last_name":"Napoli","orcid":"0000-0002-9043-136X","full_name":"Napoli, Federico"},{"first_name":"Lea Marie","last_name":"Becker","orcid":"0000-0002-6401-5151","full_name":"Becker, Lea Marie","id":"36336939-eb97-11eb-a6c2-c83f1214ca79"},{"last_name":"Schanda","first_name":"Paul","full_name":"Schanda, Paul","orcid":"0000-0002-9350-7606","id":"7B541462-FAF6-11E9-A490-E8DFE5697425"}],"issue":"10","_id":"14036","pmid":1,"scopus_import":"1","title":"Protein dynamics detected by magic-angle spinning relaxation dispersion NMR","intvolume":"        82","publication_status":"published","department":[{"_id":"PaSc"}],"article_processing_charge":"Yes (via OA deal)","date_created":"2023-08-13T22:01:11Z","status":"public","user_id":"2DF688A6-F248-11E8-B48F-1D18A9856A87","file":[{"checksum":"c850f7ac8a4234319755b672c1df69ae","file_size":1231998,"date_created":"2024-01-30T12:36:39Z","content_type":"application/pdf","file_name":"2023_CurrentOpinionStrucBio_Napoli.pdf","date_updated":"2024-01-30T12:36:39Z","relation":"main_file","success":1,"access_level":"open_access","creator":"dernst","file_id":"14907"}],"date_published":"2023-10-01T00:00:00Z","type":"journal_article","tmp":{"legal_code_url":"https://creativecommons.org/licenses/by/4.0/legalcode","short":"CC BY (4.0)","image":"/images/cc_by.png","name":"Creative Commons Attribution 4.0 International Public License (CC-BY 4.0)"},"oa":1,"publication_identifier":{"eissn":["1879-033X"],"issn":["0959-440X"]},"language":[{"iso":"eng"}],"publication":"Current Opinion in Structural Biology","month":"10","article_number":"102660","oa_version":"Published Version","project":[{"_id":"eb9c82eb-77a9-11ec-83b8-aadd536561cf","grant_number":"I05812","name":"AlloSpace. The emergence and mechanisms of allostery"}]},{"user_id":"4359f0d1-fa6c-11eb-b949-802e58b17ae8","status":"public","file":[{"success":1,"relation":"main_file","access_level":"open_access","creator":"dernst","file_id":"11725","file_size":815607,"checksum":"72bdde48853643a32d42b75f54965c44","date_created":"2022-08-05T05:56:03Z","content_type":"application/pdf","file_name":"2022_CurrentOpStructBiology_Kampjut.pdf","date_updated":"2022-08-05T05:56:03Z"}],"oa":1,"publication_identifier":{"issn":["0959-440X"]},"type":"journal_article","date_published":"2022-06-01T00:00:00Z","tmp":{"legal_code_url":"https://creativecommons.org/licenses/by/4.0/legalcode","short":"CC BY (4.0)","image":"/images/cc_by.png","name":"Creative Commons Attribution 4.0 International Public License (CC-BY 4.0)"},"keyword":["Molecular Biology","Structural Biology"],"language":[{"iso":"eng"}],"article_number":"102350","month":"06","oa_version":"Published Version","has_accepted_license":"1","publication":"Current Opinion in Structural Biology","ddc":["570"],"volume":74,"abstract":[{"lang":"eng","text":"Complex I is one of the major respiratory complexes, conserved from bacteria to mammals. It oxidises NADH, reduces quinone and pumps protons across the membrane, thus playing a central role in the oxidative energy metabolism. In this review we discuss our current state of understanding the structure of complex I from various species of mammals, plants, fungi, and bacteria, as well as of several complex I-related proteins. By comparing the structural evidence from these systems in different redox states and data from mutagenesis and molecular simulations, we formulate the mechanisms of electron transfer and proton pumping and explain how they are conformationally and electrostatically coupled. Finally, we discuss the structural basis of the deactivation phenomenon in mammalian complex I."}],"day":"01","doi":"10.1016/j.sbi.2022.102350","external_id":{"pmid":["35316665"],"isi":["000829029500020"]},"isi":1,"citation":{"short":"D. Kampjut, L.A. Sazanov, Current Opinion in Structural Biology 74 (2022).","mla":"Kampjut, Domen, and Leonid A. Sazanov. “Structure of Respiratory Complex I – An Emerging Blueprint for the Mechanism.” <i>Current Opinion in Structural Biology</i>, vol. 74, 102350, Elsevier, 2022, doi:<a href=\"https://doi.org/10.1016/j.sbi.2022.102350\">10.1016/j.sbi.2022.102350</a>.","ista":"Kampjut D, Sazanov LA. 2022. Structure of respiratory complex I – An emerging blueprint for the mechanism. Current Opinion in Structural Biology. 74, 102350.","apa":"Kampjut, D., &#38; Sazanov, L. A. (2022). Structure of respiratory complex I – An emerging blueprint for the mechanism. <i>Current Opinion in Structural Biology</i>. Elsevier. <a href=\"https://doi.org/10.1016/j.sbi.2022.102350\">https://doi.org/10.1016/j.sbi.2022.102350</a>","ama":"Kampjut D, Sazanov LA. Structure of respiratory complex I – An emerging blueprint for the mechanism. <i>Current Opinion in Structural Biology</i>. 2022;74. doi:<a href=\"https://doi.org/10.1016/j.sbi.2022.102350\">10.1016/j.sbi.2022.102350</a>","chicago":"Kampjut, Domen, and Leonid A Sazanov. “Structure of Respiratory Complex I – An Emerging Blueprint for the Mechanism.” <i>Current Opinion in Structural Biology</i>. Elsevier, 2022. <a href=\"https://doi.org/10.1016/j.sbi.2022.102350\">https://doi.org/10.1016/j.sbi.2022.102350</a>.","ieee":"D. Kampjut and L. A. Sazanov, “Structure of respiratory complex I – An emerging blueprint for the mechanism,” <i>Current Opinion in Structural Biology</i>, vol. 74. Elsevier, 2022."},"year":"2022","date_updated":"2023-08-03T06:31:06Z","article_type":"original","publisher":"Elsevier","file_date_updated":"2022-08-05T05:56:03Z","quality_controlled":"1","intvolume":"        74","title":"Structure of respiratory complex I – An emerging blueprint for the mechanism","date_created":"2022-04-15T09:32:35Z","department":[{"_id":"LeSa"}],"article_processing_charge":"Yes (via OA deal)","publication_status":"published","author":[{"id":"37233050-F248-11E8-B48F-1D18A9856A87","first_name":"Domen","last_name":"Kampjut","full_name":"Kampjut, Domen"},{"orcid":"0000-0002-0977-7989","full_name":"Sazanov, Leonid A","first_name":"Leonid A","last_name":"Sazanov","id":"338D39FE-F248-11E8-B48F-1D18A9856A87"}],"scopus_import":"1","_id":"11167","pmid":1},{"date_updated":"2023-08-25T10:13:31Z","year":"2019","citation":{"ama":"Schur FK. Toward high-resolution in situ structural biology with cryo-electron tomography and subtomogram averaging. <i>Current Opinion in Structural Biology</i>. 2019;58(10):1-9. doi:<a href=\"https://doi.org/10.1016/j.sbi.2019.03.018\">10.1016/j.sbi.2019.03.018</a>","apa":"Schur, F. K. (2019). Toward high-resolution in situ structural biology with cryo-electron tomography and subtomogram averaging. <i>Current Opinion in Structural Biology</i>. Elsevier. <a href=\"https://doi.org/10.1016/j.sbi.2019.03.018\">https://doi.org/10.1016/j.sbi.2019.03.018</a>","ieee":"F. K. Schur, “Toward high-resolution in situ structural biology with cryo-electron tomography and subtomogram averaging,” <i>Current Opinion in Structural Biology</i>, vol. 58, no. 10. Elsevier, pp. 1–9, 2019.","chicago":"Schur, Florian KM. “Toward High-Resolution in Situ Structural Biology with Cryo-Electron Tomography and Subtomogram Averaging.” <i>Current Opinion in Structural Biology</i>. Elsevier, 2019. <a href=\"https://doi.org/10.1016/j.sbi.2019.03.018\">https://doi.org/10.1016/j.sbi.2019.03.018</a>.","mla":"Schur, Florian KM. “Toward High-Resolution in Situ Structural Biology with Cryo-Electron Tomography and Subtomogram Averaging.” <i>Current Opinion in Structural Biology</i>, vol. 58, no. 10, Elsevier, 2019, pp. 1–9, doi:<a href=\"https://doi.org/10.1016/j.sbi.2019.03.018\">10.1016/j.sbi.2019.03.018</a>.","short":"F.K. Schur, Current Opinion in Structural Biology 58 (2019) 1–9.","ista":"Schur FK. 2019. Toward high-resolution in situ structural biology with cryo-electron tomography and subtomogram averaging. Current Opinion in Structural Biology. 58(10), 1–9."},"isi":1,"external_id":{"isi":["000494891800004"]},"doi":"10.1016/j.sbi.2019.03.018","day":"01","abstract":[{"lang":"eng","text":"Cryo-electron tomography (cryo-ET) provides unprecedented insights into the molecular constituents of biological environments. In combination with an image processing method called subtomogram averaging (STA), detailed 3D structures of biological molecules can be obtained in large, irregular macromolecular assemblies or in situ, without the need for purification. The contextual meta-information these methods also provide, such as a protein’s location within its native environment, can then be combined with functional data. This allows the derivation of a detailed view on the physiological or pathological roles of proteins from the molecular to cellular level. Despite their tremendous potential in in situ structural biology, cryo-ET and STA have been restricted by methodological limitations, such as the low obtainable resolution. Exciting progress now allows one to reach unprecedented resolutions in situ, ranging in optimal cases beyond the nanometer barrier. Here, I review current frontiers and future challenges in routinely determining high-resolution structures in in situ environments using cryo-ET and STA."}],"acknowledgement":"The author acknowledges support from IST Austria and the Austrian Science Fund (FWF).","volume":58,"_id":"6343","scopus_import":"1","author":[{"last_name":"Schur","first_name":"Florian KM","full_name":"Schur, Florian KM","orcid":"0000-0003-4790-8078","id":"48AD8942-F248-11E8-B48F-1D18A9856A87"}],"issue":"10","publication_status":"published","department":[{"_id":"FlSc"}],"date_created":"2019-04-19T11:19:13Z","article_processing_charge":"No","title":"Toward high-resolution in situ structural biology with cryo-electron tomography and subtomogram averaging","intvolume":"        58","page":"1-9","quality_controlled":"1","publisher":"Elsevier","article_type":"original","date_published":"2019-10-01T00:00:00Z","type":"journal_article","publication_identifier":{"issn":["0959-440X"]},"status":"public","user_id":"4359f0d1-fa6c-11eb-b949-802e58b17ae8","publication":"Current Opinion in Structural Biology","oa_version":"None","month":"10","language":[{"iso":"eng"}]},{"extern":"1","volume":58,"acknowledgement":"We acknowledge funding from EPSRC (A.E.H. and A.Š.), the Academy of Medical Sciences (J.K. and A.Š.), the Wellcome Trust (J.K. and A.Š.), and the Royal Society (A.Š.). We thank Shiladitya Banerjee and Nikola Ojkic for critically reading the manuscript, and Claudia Flandoli for helping us with figures and illustrations.","abstract":[{"text":"The molecular machinery of life is largely created via self-organisation of individual molecules into functional assemblies. Minimal coarse-grained models, in which a whole macromolecule is represented by a small number of particles, can be of great value in identifying the main driving forces behind self-organisation in cell biology. Such models can incorporate data from both molecular and continuum scales, and their results can be directly compared to experiments. Here we review the state of the art of models for studying the formation and biological function of macromolecular assemblies in living organisms. We outline the key ingredients of each model and their main findings. We illustrate the contribution of this class of simulations to identifying the physical mechanisms behind life and diseases, and discuss their future developments.","lang":"eng"}],"day":"18","doi":"10.1016/j.sbi.2019.05.018","external_id":{"pmid":["31226513"]},"citation":{"ama":"Hafner AE, Krausser J, Šarić A. Minimal coarse-grained models for molecular self-organisation in biology. <i>Current Opinion in Structural Biology</i>. 2019;58:43-52. doi:<a href=\"https://doi.org/10.1016/j.sbi.2019.05.018\">10.1016/j.sbi.2019.05.018</a>","apa":"Hafner, A. E., Krausser, J., &#38; Šarić, A. (2019). Minimal coarse-grained models for molecular self-organisation in biology. <i>Current Opinion in Structural Biology</i>. Elsevier. <a href=\"https://doi.org/10.1016/j.sbi.2019.05.018\">https://doi.org/10.1016/j.sbi.2019.05.018</a>","chicago":"Hafner, Anne E, Johannes Krausser, and Anđela Šarić. “Minimal Coarse-Grained Models for Molecular Self-Organisation in Biology.” <i>Current Opinion in Structural Biology</i>. Elsevier, 2019. <a href=\"https://doi.org/10.1016/j.sbi.2019.05.018\">https://doi.org/10.1016/j.sbi.2019.05.018</a>.","ieee":"A. E. Hafner, J. Krausser, and A. Šarić, “Minimal coarse-grained models for molecular self-organisation in biology,” <i>Current Opinion in Structural Biology</i>, vol. 58. Elsevier, pp. 43–52, 2019.","mla":"Hafner, Anne E., et al. “Minimal Coarse-Grained Models for Molecular Self-Organisation in Biology.” <i>Current Opinion in Structural Biology</i>, vol. 58, Elsevier, 2019, pp. 43–52, doi:<a href=\"https://doi.org/10.1016/j.sbi.2019.05.018\">10.1016/j.sbi.2019.05.018</a>.","short":"A.E. Hafner, J. Krausser, A. Šarić, Current Opinion in Structural Biology 58 (2019) 43–52.","ista":"Hafner AE, Krausser J, Šarić A. 2019. Minimal coarse-grained models for molecular self-organisation in biology. Current Opinion in Structural Biology. 58, 43–52."},"year":"2019","date_updated":"2021-11-26T11:54:25Z","article_type":"original","publisher":"Elsevier","quality_controlled":"1","page":"43-52","intvolume":"        58","title":"Minimal coarse-grained models for molecular self-organisation in biology","article_processing_charge":"No","date_created":"2021-11-26T11:33:21Z","publication_status":"published","author":[{"full_name":"Hafner, Anne E","first_name":"Anne E","last_name":"Hafner"},{"full_name":"Krausser, Johannes","first_name":"Johannes","last_name":"Krausser"},{"first_name":"Anđela","last_name":"Šarić","orcid":"0000-0002-7854-2139","full_name":"Šarić, Anđela","id":"bf63d406-f056-11eb-b41d-f263a6566d8b"}],"scopus_import":"1","_id":"10355","pmid":1,"user_id":"8b945eb4-e2f2-11eb-945a-df72226e66a9","status":"public","main_file_link":[{"url":"https://arxiv.org/abs/1906.09349","open_access":"1"}],"oa":1,"publication_identifier":{"issn":["0959-440X"]},"type":"journal_article","date_published":"2019-06-18T00:00:00Z","keyword":["molecular biology","structural biology"],"language":[{"iso":"eng"}],"month":"06","oa_version":"Preprint","publication":"Current Opinion in Structural Biology"}]