[{"file_date_updated":"2024-01-23T08:57:01Z","date_created":"2024-01-18T10:01:01Z","volume":135,"month":"05","type":"journal_article","oa_version":"Published Version","abstract":[{"lang":"ger","text":"Aromatische Seitenketten sind wichtige Indikatoren für die Plastizität von Proteinen und bilden oft entscheidende Kontakte bei Protein‐Protein‐Wechselwirkungen. Wir untersuchten aromatische Reste in den beiden strukturell homologen cross‐β Amyloidfibrillen HET‐s und HELLF mit Hilfe eines spezifischen Ansatzes zur Isotopenmarkierung und Festkörper NMR mit Drehung am magischen Winkel. Das dynamische Verhalten der aromatischen Reste Phe und Tyr deutet darauf hin, dass der hydrophobe Amyloidkern starr ist und keine Anzeichen von “atmenden Bewegungen” auf einer Zeitskala von Hunderten von Millisekunden zeigt. Aromatische Reste, die exponiert an der Fibrillenoberfläche sitzen, haben zwar eine starre Ringachse, weisen aber Ringflips auf verschiedenen Zeitskalen von Nanosekunden bis Mikrosekunden auf. Unser Ansatz bietet einen direkten Einblick in die Bewegungen des hydrophoben Kerns und ermöglicht eine bessere Bewertung der Konformationsheterogenität, die aus einem NMR‐Strukturensemble einer solchen Cross‐β‐Amyloidstruktur hervorgeht."}],"date_updated":"2024-01-23T12:23:35Z","_id":"14835","year":"2023","acknowledgement":"Wir danken Albert A. Smith (Leipzig) für aufschlussreiche Diskussionen. Diese Arbeit wurde mit Mitteln des Europäischen Forschungsrats (StG-2012-311318 an P.S.) unterstützt und nutzte die Plattformen des Grenoble Instruct-ERIC Center (ISBG; UMS 3518 CNRS-CEA-UJF-EMBL) im Rahmen der Grenoble Partnership for Structural Biology (PSB) sowie die Einrichtungen und das Fachwissen der Biophysical and Structural Chemistry Platform (BPCS) am IECB, CNRS UAR3033, INSERM US001 und der Universität Bordeaux.","date_published":"2023-05-02T00:00:00Z","ddc":["540"],"has_accepted_license":"1","oa":1,"publication_status":"published","citation":{"chicago":"Becker, Lea Marie, Mélanie Berbon, Alicia Vallet, Axelle Grelard, Estelle Morvan, Benjamin Bardiaux, Roman Lichtenecker, Matthias Ernst, Antoine Loquet, and Paul Schanda. “Der starre Kern und die flexible Oberfläche von Amyloidfibrillen – Magic‐Angle‐Spinning NMR Spektroskopie von aromatischen Resten.” <i>Angewandte Chemie</i>. Wiley, 2023. <a href=\"https://doi.org/10.1002/ange.202219314\">https://doi.org/10.1002/ange.202219314</a>.","ieee":"L. M. Becker <i>et al.</i>, “Der starre Kern und die flexible Oberfläche von Amyloidfibrillen – Magic‐Angle‐Spinning NMR Spektroskopie von aromatischen Resten,” <i>Angewandte Chemie</i>, vol. 135, no. 19. Wiley, 2023.","short":"L.M. Becker, M. Berbon, A. Vallet, A. Grelard, E. Morvan, B. Bardiaux, R. Lichtenecker, M. Ernst, A. Loquet, P. Schanda, Angewandte Chemie 135 (2023).","ama":"Becker LM, Berbon M, Vallet A, et al. Der starre Kern und die flexible Oberfläche von Amyloidfibrillen – Magic‐Angle‐Spinning NMR Spektroskopie von aromatischen Resten. <i>Angewandte Chemie</i>. 2023;135(19). doi:<a href=\"https://doi.org/10.1002/ange.202219314\">10.1002/ange.202219314</a>","apa":"Becker, L. M., Berbon, M., Vallet, A., Grelard, A., Morvan, E., Bardiaux, B., … Schanda, P. (2023). Der starre Kern und die flexible Oberfläche von Amyloidfibrillen – Magic‐Angle‐Spinning NMR Spektroskopie von aromatischen Resten. <i>Angewandte Chemie</i>. Wiley. <a href=\"https://doi.org/10.1002/ange.202219314\">https://doi.org/10.1002/ange.202219314</a>","mla":"Becker, Lea Marie, et al. “Der starre Kern und die flexible Oberfläche von Amyloidfibrillen – Magic‐Angle‐Spinning NMR Spektroskopie von aromatischen Resten.” <i>Angewandte Chemie</i>, vol. 135, no. 19, e202219314, Wiley, 2023, doi:<a href=\"https://doi.org/10.1002/ange.202219314\">10.1002/ange.202219314</a>.","ista":"Becker LM, Berbon M, Vallet A, Grelard A, Morvan E, Bardiaux B, Lichtenecker R, Ernst M, Loquet A, Schanda P. 2023. Der starre Kern und die flexible Oberfläche von Amyloidfibrillen – Magic‐Angle‐Spinning NMR Spektroskopie von aromatischen Resten. Angewandte Chemie. 135(19), e202219314."},"intvolume":"       135","status":"public","article_number":"e202219314","title":"Der starre Kern und die flexible Oberfläche von Amyloidfibrillen – Magic‐Angle‐Spinning NMR Spektroskopie von aromatischen Resten","file":[{"success":1,"file_name":"2023_AngewChem_Becker.pdf","creator":"dernst","relation":"main_file","content_type":"application/pdf","file_size":1004676,"checksum":"98e68d370159f7be52a3d7c8a8ee1198","date_updated":"2024-01-23T08:57:01Z","file_id":"14876","access_level":"open_access","date_created":"2024-01-23T08:57:01Z"}],"day":"02","author":[{"last_name":"Becker","first_name":"Lea Marie","orcid":"0000-0002-6401-5151","id":"36336939-eb97-11eb-a6c2-c83f1214ca79","full_name":"Becker, Lea Marie"},{"first_name":"Mélanie","last_name":"Berbon","full_name":"Berbon, Mélanie"},{"full_name":"Vallet, Alicia","last_name":"Vallet","first_name":"Alicia"},{"full_name":"Grelard, Axelle","first_name":"Axelle","last_name":"Grelard"},{"full_name":"Morvan, Estelle","first_name":"Estelle","last_name":"Morvan"},{"full_name":"Bardiaux, Benjamin","first_name":"Benjamin","last_name":"Bardiaux"},{"full_name":"Lichtenecker, Roman","last_name":"Lichtenecker","first_name":"Roman"},{"first_name":"Matthias","last_name":"Ernst","full_name":"Ernst, Matthias"},{"full_name":"Loquet, Antoine","last_name":"Loquet","first_name":"Antoine"},{"orcid":"0000-0002-9350-7606","id":"7B541462-FAF6-11E9-A490-E8DFE5697425","full_name":"Schanda, Paul","first_name":"Paul","last_name":"Schanda"}],"article_type":"original","tmp":{"name":"Creative Commons Attribution-NonCommercial 4.0 International (CC BY-NC 4.0)","short":"CC BY-NC (4.0)","image":"/images/cc_by_nc.png","legal_code_url":"https://creativecommons.org/licenses/by-nc/4.0/legalcode"},"article_processing_charge":"Yes (in subscription journal)","publication":"Angewandte Chemie","department":[{"_id":"PaSc"}],"publisher":"Wiley","user_id":"2DF688A6-F248-11E8-B48F-1D18A9856A87","quality_controlled":"1","doi":"10.1002/ange.202219314","publication_identifier":{"issn":["0044-8249"],"eissn":["1521-3757"]},"issue":"19","language":[{"iso":"ger"}],"keyword":["General Medicine"]},{"related_material":{"link":[{"relation":"translation","url":"https://doi.org/10.1002/ange.202304138"}],"record":[{"status":"public","id":"12675","relation":"other"}]},"intvolume":"        62","citation":{"short":"L.M. Becker, M. Berbon, A. Vallet, A. Grelard, E. Morvan, B. Bardiaux, R. Lichtenecker, M. Ernst, A. Loquet, P. Schanda, Cover Picture: The Rigid Core and Flexible Surface of Amyloid Fibrils Probed by Magic‐Angle‐Spinning NMR Spectroscopy of Aromatic Residues, Wiley, 2023.","ieee":"L. M. Becker <i>et al.</i>, <i>Cover Picture: The rigid core and flexible surface of amyloid fibrils probed by Magic‐Angle‐Spinning NMR spectroscopy of aromatic residues</i>, vol. 62, no. 19. Wiley, 2023.","chicago":"Becker, Lea Marie, Mélanie Berbon, Alicia Vallet, Axelle Grelard, Estelle Morvan, Benjamin Bardiaux, Roman Lichtenecker, Matthias Ernst, Antoine Loquet, and Paul Schanda. <i>Cover Picture: The Rigid Core and Flexible Surface of Amyloid Fibrils Probed by Magic‐Angle‐Spinning NMR Spectroscopy of Aromatic Residues</i>. <i>Angewandte Chemie International Edition</i>. Vol. 62. Wiley, 2023. <a href=\"https://doi.org/10.1002/anie.202304138\">https://doi.org/10.1002/anie.202304138</a>.","mla":"Becker, Lea Marie, et al. “Cover Picture: The Rigid Core and Flexible Surface of Amyloid Fibrils Probed by Magic‐Angle‐Spinning NMR Spectroscopy of Aromatic Residues.” <i>Angewandte Chemie International Edition</i>, vol. 62, no. 19, e202304138, Wiley, 2023, doi:<a href=\"https://doi.org/10.1002/anie.202304138\">10.1002/anie.202304138</a>.","ista":"Becker LM, Berbon M, Vallet A, Grelard A, Morvan E, Bardiaux B, Lichtenecker R, Ernst M, Loquet A, Schanda P. 2023. Cover Picture: The rigid core and flexible surface of amyloid fibrils probed by Magic‐Angle‐Spinning NMR spectroscopy of aromatic residues, Wiley,p.","apa":"Becker, L. M., Berbon, M., Vallet, A., Grelard, A., Morvan, E., Bardiaux, B., … Schanda, P. (2023). <i>Cover Picture: The rigid core and flexible surface of amyloid fibrils probed by Magic‐Angle‐Spinning NMR spectroscopy of aromatic residues</i>. <i>Angewandte Chemie International Edition</i> (Vol. 62). Wiley. <a href=\"https://doi.org/10.1002/anie.202304138\">https://doi.org/10.1002/anie.202304138</a>","ama":"Becker LM, Berbon M, Vallet A, et al. <i>Cover Picture: The Rigid Core and Flexible Surface of Amyloid Fibrils Probed by Magic‐Angle‐Spinning NMR Spectroscopy of Aromatic Residues</i>. Vol 62. Wiley; 2023. doi:<a href=\"https://doi.org/10.1002/anie.202304138\">10.1002/anie.202304138</a>"},"status":"public","date_published":"2023-05-02T00:00:00Z","main_file_link":[{"url":"https://doi.org/10.1002/anie.202304138","open_access":"1"}],"oa":1,"publication_status":"published","_id":"14861","year":"2023","volume":62,"date_created":"2024-01-22T11:54:34Z","abstract":[{"text":"Cover Page","lang":"eng"}],"date_updated":"2024-01-23T08:48:14Z","type":"other_academic_publication","month":"05","oa_version":"Published Version","keyword":["General Chemistry","Catalysis"],"language":[{"iso":"eng"}],"issue":"19","doi":"10.1002/anie.202304138","publication_identifier":{"issn":["1433-7851"],"eissn":["1521-3773"]},"publication":"Angewandte Chemie International Edition","article_processing_charge":"No","publisher":"Wiley","user_id":"2DF688A6-F248-11E8-B48F-1D18A9856A87","department":[{"_id":"PaSc"}],"title":"Cover Picture: The rigid core and flexible surface of amyloid fibrils probed by Magic‐Angle‐Spinning NMR spectroscopy of aromatic residues","article_number":" e202304138","author":[{"id":"36336939-eb97-11eb-a6c2-c83f1214ca79","orcid":"0000-0002-6401-5151","full_name":"Becker, Lea Marie","first_name":"Lea Marie","last_name":"Becker"},{"full_name":"Berbon, Mélanie","last_name":"Berbon","first_name":"Mélanie"},{"last_name":"Vallet","first_name":"Alicia","full_name":"Vallet, Alicia"},{"full_name":"Grelard, Axelle","last_name":"Grelard","first_name":"Axelle"},{"first_name":"Estelle","last_name":"Morvan","full_name":"Morvan, Estelle"},{"last_name":"Bardiaux","first_name":"Benjamin","full_name":"Bardiaux, Benjamin"},{"full_name":"Lichtenecker, Roman","last_name":"Lichtenecker","first_name":"Roman"},{"first_name":"Matthias","last_name":"Ernst","full_name":"Ernst, Matthias"},{"full_name":"Loquet, Antoine","first_name":"Antoine","last_name":"Loquet"},{"orcid":"0000-0002-9350-7606","id":"7B541462-FAF6-11E9-A490-E8DFE5697425","full_name":"Schanda, Paul","last_name":"Schanda","first_name":"Paul"}],"day":"02"},{"oa":1,"publication_status":"published","ddc":["570"],"date_published":"2023-10-01T00:00:00Z","external_id":{"pmid":["37536064"],"isi":["001053616200001"]},"status":"public","intvolume":"        82","citation":{"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>","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>.","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>","short":"F. Napoli, L.M. Becker, P. Schanda, Current Opinion in Structural Biology 82 (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>.","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."},"month":"10","oa_version":"Published Version","type":"journal_article","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"}],"date_updated":"2024-01-30T12:37:36Z","volume":82,"date_created":"2023-08-13T22:01:11Z","file_date_updated":"2024-01-30T12:36:39Z","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.","year":"2023","_id":"14036","publication_identifier":{"eissn":["1879-033X"],"issn":["0959-440X"]},"doi":"10.1016/j.sbi.2023.102660","quality_controlled":"1","project":[{"grant_number":"I05812","name":"AlloSpace. The emergence and mechanisms of allostery","_id":"eb9c82eb-77a9-11ec-83b8-aadd536561cf"}],"isi":1,"issue":"10","language":[{"iso":"eng"}],"author":[{"first_name":"Federico","last_name":"Napoli","id":"d42e08e7-f4fc-11eb-af0a-d71e26138f1b","orcid":"0000-0002-9043-136X","full_name":"Napoli, Federico"},{"id":"36336939-eb97-11eb-a6c2-c83f1214ca79","orcid":"0000-0002-6401-5151","full_name":"Becker, Lea Marie","first_name":"Lea Marie","last_name":"Becker"},{"full_name":"Schanda, Paul","orcid":"0000-0002-9350-7606","id":"7B541462-FAF6-11E9-A490-E8DFE5697425","last_name":"Schanda","first_name":"Paul"}],"day":"01","file":[{"file_id":"14907","date_updated":"2024-01-30T12:36:39Z","checksum":"c850f7ac8a4234319755b672c1df69ae","date_created":"2024-01-30T12:36:39Z","access_level":"open_access","file_name":"2023_CurrentOpinionStrucBio_Napoli.pdf","success":1,"file_size":1231998,"content_type":"application/pdf","relation":"main_file","creator":"dernst"}],"article_number":"102660","title":"Protein dynamics detected by magic-angle spinning relaxation dispersion NMR","user_id":"2DF688A6-F248-11E8-B48F-1D18A9856A87","publisher":"Elsevier","department":[{"_id":"PaSc"}],"pmid":1,"publication":"Current Opinion in Structural Biology","tmp":{"legal_code_url":"https://creativecommons.org/licenses/by/4.0/legalcode","image":"/images/cc_by.png","name":"Creative Commons Attribution 4.0 International Public License (CC-BY 4.0)","short":"CC BY (4.0)"},"article_type":"original","scopus_import":"1","article_processing_charge":"Yes (via OA deal)"},{"external_id":{"pmid":["36578472"]},"status":"public","intvolume":"         7","citation":{"short":"D.F. Gauto, O.O. Lebedenko, L.M. Becker, I. Ayala, R. Lichtenecker, N.R. Skrynnikov, P. Schanda, Journal of Structural Biology: X 7 (2023).","chicago":"Gauto, Diego F., Olga O. Lebedenko, Lea Marie Becker, Isabel Ayala, Roman Lichtenecker, Nikolai R. Skrynnikov, and Paul Schanda. “Aromatic Ring Flips in Differently Packed Ubiquitin Protein Crystals from MAS NMR and MD.” <i>Journal of Structural Biology: X</i>. Elsevier, 2023. <a href=\"https://doi.org/10.1016/j.yjsbx.2022.100079\">https://doi.org/10.1016/j.yjsbx.2022.100079</a>.","ieee":"D. F. Gauto <i>et al.</i>, “Aromatic ring flips in differently packed ubiquitin protein crystals from MAS NMR and MD,” <i>Journal of Structural Biology: X</i>, vol. 7. Elsevier, 2023.","apa":"Gauto, D. F., Lebedenko, O. O., Becker, L. M., Ayala, I., Lichtenecker, R., Skrynnikov, N. R., &#38; Schanda, P. (2023). Aromatic ring flips in differently packed ubiquitin protein crystals from MAS NMR and MD. <i>Journal of Structural Biology: X</i>. Elsevier. <a href=\"https://doi.org/10.1016/j.yjsbx.2022.100079\">https://doi.org/10.1016/j.yjsbx.2022.100079</a>","mla":"Gauto, Diego F., et al. “Aromatic Ring Flips in Differently Packed Ubiquitin Protein Crystals from MAS NMR and MD.” <i>Journal of Structural Biology: X</i>, vol. 7, 100079, Elsevier, 2023, doi:<a href=\"https://doi.org/10.1016/j.yjsbx.2022.100079\">10.1016/j.yjsbx.2022.100079</a>.","ista":"Gauto DF, Lebedenko OO, Becker LM, Ayala I, Lichtenecker R, Skrynnikov NR, Schanda P. 2023. Aromatic ring flips in differently packed ubiquitin protein crystals from MAS NMR and MD. Journal of Structural Biology: X. 7, 100079.","ama":"Gauto DF, Lebedenko OO, Becker LM, et al. Aromatic ring flips in differently packed ubiquitin protein crystals from MAS NMR and MD. <i>Journal of Structural Biology: X</i>. 2023;7. doi:<a href=\"https://doi.org/10.1016/j.yjsbx.2022.100079\">10.1016/j.yjsbx.2022.100079</a>"},"publication_status":"published","oa":1,"has_accepted_license":"1","date_published":"2023-01-01T00:00:00Z","ddc":["570"],"acknowledgement":"The NMR platform in Grenoble is part of the Grenoble Instruct-ERIC center (ISBG; UAR 3518 CNRS-CEA-UGA-EMBL) within the Grenoble Partnership for Structural Biology (PSB), supported by FRISBI (ANR-10-INBS-0005-02) and GRAL, financed within the University Grenoble Alpes graduate school (Ecoles Universitaires de Recherche) CBH-EUR-GS (ANR-17-EURE-0003). This work was supported by the European Research Council (StG-2012-311318-ProtDyn2Function to P.S.) and used the platforms of the Grenoble Instruct Center (ISBG; UMS 3518 CNRS-CEA-UJF-EMBL) with support from FRISBI (ANR-10-INSB-05–02) and GRAL (ANR-10-LABX-49–01) within the Grenoble Partnership for Structural Biology (PSB). We would like to thank Sergei Izmailov for developing and maintaining the pyxmolpp2 library. N.R.S. acknowledges support from St. Petersburg State University in a form of the grant 92425251 and the access to the MRR, MCT and CAMR resource centers. P.S. thanks Malcolm Levitt for pointing out the fact that “tensor asymmetry” is better called “tensor biaxiality”.","year":"2023","_id":"12114","date_updated":"2023-08-16T09:37:25Z","abstract":[{"lang":"eng","text":"Probing the dynamics of aromatic side chains provides important insights into the behavior of a protein because flips of aromatic rings in a protein’s hydrophobic core report on breathing motion involving a large part of the protein. Inherently invisible to crystallography, aromatic motions have been primarily studied by solution NMR. The question how packing of proteins in crystals affects ring flips has, thus, remained largely unexplored. Here we apply magic-angle spinning NMR, advanced phenylalanine 1H-13C/2H isotope labeling and MD simulation to a protein in three different crystal packing environments to shed light onto possible impact of packing on ring flips. The flips of the two Phe residues in ubiquitin, both surface exposed, appear remarkably conserved in the different crystal forms, even though the intermolecular packing is quite different: Phe4 flips on a ca. 10–20 ns time scale, and Phe45 are broadened in all crystals, presumably due to µs motion. Our findings suggest that intramolecular influences are more important for ring flips than intermolecular (packing) effects."}],"month":"01","oa_version":"Published Version","type":"journal_article","volume":7,"file_date_updated":"2023-08-16T09:36:28Z","date_created":"2023-01-12T11:55:38Z","keyword":["Structural Biology"],"language":[{"iso":"eng"}],"publication_identifier":{"issn":["2590-1524"]},"doi":"10.1016/j.yjsbx.2022.100079","quality_controlled":"1","user_id":"2DF688A6-F248-11E8-B48F-1D18A9856A87","publisher":"Elsevier","pmid":1,"department":[{"_id":"PaSc"}],"publication":"Journal of Structural Biology: X","scopus_import":"1","article_processing_charge":"No","article_type":"original","tmp":{"name":"Creative Commons Attribution-NonCommercial-NoDerivatives 4.0 International (CC BY-NC-ND 4.0)","short":"CC BY-NC-ND (4.0)","image":"/images/cc_by_nc_nd.png","legal_code_url":"https://creativecommons.org/licenses/by-nc-nd/4.0/legalcode"},"author":[{"first_name":"Diego F.","last_name":"Gauto","full_name":"Gauto, Diego F."},{"full_name":"Lebedenko, Olga O.","last_name":"Lebedenko","first_name":"Olga O."},{"first_name":"Lea Marie","last_name":"Becker","orcid":"0000-0002-6401-5151","id":"36336939-eb97-11eb-a6c2-c83f1214ca79","full_name":"Becker, Lea Marie"},{"first_name":"Isabel","last_name":"Ayala","full_name":"Ayala, Isabel"},{"last_name":"Lichtenecker","first_name":"Roman","full_name":"Lichtenecker, Roman"},{"first_name":"Nikolai R.","last_name":"Skrynnikov","full_name":"Skrynnikov, Nikolai R."},{"first_name":"Paul","last_name":"Schanda","id":"7B541462-FAF6-11E9-A490-E8DFE5697425","orcid":"0000-0002-9350-7606","full_name":"Schanda, Paul"}],"day":"01","file":[{"date_created":"2023-08-16T09:36:28Z","access_level":"open_access","file_id":"14064","date_updated":"2023-08-16T09:36:28Z","checksum":"b4b1c10a31018aafe053b7d55a470e54","file_size":5132322,"content_type":"application/pdf","relation":"main_file","creator":"dernst","file_name":"2023_JourStrucBiologyX_Gauto.pdf","success":1}],"title":"Aromatic ring flips in differently packed ubiquitin protein crystals from MAS NMR and MD","article_number":"100079"},{"status":"public","keyword":["aromatic side chains","isotopic labeling","protein dynamics","ring flips","spin relaxation"],"related_material":{"record":[{"relation":"used_in_publication","status":"public","id":"12675"}]},"citation":{"short":"L.M. Becker, P. Schanda, (2023).","ieee":"L. M. Becker and P. Schanda, “Research data to: The rigid core and flexible surface of amyloid fibrils probed by magic-angle-spinning NMR spectroscopy of aromatic residues.” Institute of Science and Technology Austria, 2023.","chicago":"Becker, Lea Marie, and Paul Schanda. “Research Data to: The Rigid Core and Flexible Surface of Amyloid Fibrils Probed by Magic-Angle-Spinning NMR Spectroscopy of Aromatic Residues.” Institute of Science and Technology Austria, 2023. <a href=\"https://doi.org/10.15479/AT:ISTA:12497\">https://doi.org/10.15479/AT:ISTA:12497</a>.","mla":"Becker, Lea Marie, and Paul Schanda. <i>Research Data to: The Rigid Core and Flexible Surface of Amyloid Fibrils Probed by Magic-Angle-Spinning NMR Spectroscopy of Aromatic Residues</i>. Institute of Science and Technology Austria, 2023, doi:<a href=\"https://doi.org/10.15479/AT:ISTA:12497\">10.15479/AT:ISTA:12497</a>.","ista":"Becker LM, Schanda P. 2023. Research data to: The rigid core and flexible surface of amyloid fibrils probed by magic-angle-spinning NMR spectroscopy of aromatic residues, Institute of Science and Technology Austria, <a href=\"https://doi.org/10.15479/AT:ISTA:12497\">10.15479/AT:ISTA:12497</a>.","apa":"Becker, L. M., &#38; Schanda, P. (2023). Research data to: The rigid core and flexible surface of amyloid fibrils probed by magic-angle-spinning NMR spectroscopy of aromatic residues. Institute of Science and Technology Austria. <a href=\"https://doi.org/10.15479/AT:ISTA:12497\">https://doi.org/10.15479/AT:ISTA:12497</a>","ama":"Becker LM, Schanda P. Research data to: The rigid core and flexible surface of amyloid fibrils probed by magic-angle-spinning NMR spectroscopy of aromatic residues. 2023. doi:<a href=\"https://doi.org/10.15479/AT:ISTA:12497\">10.15479/AT:ISTA:12497</a>"},"oa":1,"has_accepted_license":"1","contributor":[{"last_name":"Berbon","contributor_type":"researcher","first_name":"Mélanie"},{"last_name":"Vallet","contributor_type":"researcher","first_name":"Alicia"},{"contributor_type":"researcher","first_name":"Axelle","last_name":"Grelard"},{"last_name":"Morvan","contributor_type":"researcher","first_name":"Estelle"},{"first_name":"Benjamin","contributor_type":"researcher","last_name":"Bardiaux"},{"first_name":"Roman","contributor_type":"researcher","last_name":"Lichtenecker"},{"last_name":"Ernst","contributor_type":"researcher","first_name":"Matthias"},{"first_name":"Antoine","contributor_type":"researcher","last_name":"Loquet"},{"last_name":"Schanda","first_name":"Paul","contributor_type":"contact_person","id":"7B541462-FAF6-11E9-A490-E8DFE5697425","orcid":"0000-0002-9350-7606"},{"contributor_type":"researcher","first_name":"Lea Marie","last_name":"Becker","orcid":"0000-0002-6401-5151","id":"36336939-eb97-11eb-a6c2-c83f1214ca79"}],"date_published":"2023-03-23T00:00:00Z","doi":"10.15479/AT:ISTA:12497","ddc":["572"],"user_id":"2DF688A6-F248-11E8-B48F-1D18A9856A87","publisher":"Institute of Science and Technology Austria","year":"2023","department":[{"_id":"GradSch"},{"_id":"PaSc"}],"_id":"12497","tmp":{"name":"Creative Commons Attribution-NonCommercial 4.0 International (CC BY-NC 4.0)","short":"CC BY-NC (4.0)","image":"/images/cc_by_nc.png","legal_code_url":"https://creativecommons.org/licenses/by-nc/4.0/legalcode"},"article_processing_charge":"No","author":[{"first_name":"Lea Marie","last_name":"Becker","orcid":"0000-0002-6401-5151","id":"36336939-eb97-11eb-a6c2-c83f1214ca79","full_name":"Becker, Lea Marie"},{"first_name":"Paul","last_name":"Schanda","full_name":"Schanda, Paul","orcid":"0000-0002-9350-7606","id":"7B541462-FAF6-11E9-A490-E8DFE5697425"}],"oa_version":"Published Version","type":"research_data","month":"03","file":[{"relation":"main_file","content_type":"application/zip","file_size":87018103,"creator":"lbecker","file_name":"Research_Data.zip","date_created":"2023-03-23T10:03:16Z","access_level":"open_access","date_updated":"2023-03-24T09:34:20Z","file_id":"12743","checksum":"fd9a28620a81a82991fb70f4fd6591d9"},{"file_name":"README.txt","creator":"dernst","file_size":747,"relation":"main_file","content_type":"text/plain","checksum":"30ebdfb600af118fcf8518b6efe0b7e9","file_id":"12755","date_updated":"2023-03-24T09:42:03Z","access_level":"open_access","date_created":"2023-03-24T07:13:55Z"}],"abstract":[{"text":"Aromatic side chains are important reporters of the plasticity of proteins, and often form important contacts in protein–protein interactions. We studied aromatic residues in the two structurally homologous cross-β amyloid fibrils HET-s, and  HELLF by employing a specific isotope-labeling approach and magic-angle-spinning NMR. The dynamic behavior of the aromatic residues Phe and Tyr indicates that the hydrophobic amyloid core is rigid, without any sign of \"breathing motions\" over hundreds of milliseconds at least. Aromatic residues exposed at the fibril surface have a rigid ring axis but undergo ring flips on a variety of time scales from nanoseconds to microseconds. Our approach provides direct insight into hydrophobic-core motions, enabling a better evaluation of the conformational heterogeneity generated from an NMR structural ensemble of such amyloid cross-β architecture.","lang":"eng"}],"day":"23","date_updated":"2024-02-21T12:14:06Z","title":"Research data to: The rigid core and flexible surface of amyloid fibrils probed by magic-angle-spinning NMR spectroscopy of aromatic residues","date_created":"2023-02-03T08:08:02Z","file_date_updated":"2023-03-24T09:42:03Z"},{"year":"2023","acknowledgement":"We thank AlbertA. Smith (Leipzig)for insightful discussions. This work was supported by funding from the European Research Council (StG-2012-311318 to P.S.) and used the platforms of the Grenoble Instruct-ERIC center (ISBG;UMS 3518 CNRS-CEA-UJF-EMBL) within the Grenoble Partnership for Structural Biology(PSB) and facilities and expertiseof the Biophysical and Structural Chemistry platform (BPCS) at IECB,CNRSUAR3033,INSERMUS001 and Bordeaux University.","_id":"12675","oa_version":"Published Version","month":"05","type":"journal_article","abstract":[{"text":"Aromatic side chains are important reporters of the plasticity of proteins, and often form important contacts in protein--protein interactions. By studying a pair of structurally homologous cross-β amyloid fibrils, HET-s and HELLF, with a specific isotope-labeling approach and magic-angle-spinning (MAS) NMR, we have characterized the dynamic behavior of Phe and Tyr aromatic rings to show that the hydrophobic amyloid core is rigid, without any sign of \"breathing motions\" over hundreds of milliseconds at least. Aromatic residues exposed at the fibril surface have a rigid ring axis but undergo ring flips, on a variety of time scales from ns to µs. Our approach provides direct insight into hydrophobic-core motions, enabling a better evaluation of the conformational heterogeneity generated from a NMR structural ensemble of such amyloid cross-β architecture.","lang":"eng"}],"date_updated":"2024-02-21T12:14:06Z","file_date_updated":"2023-08-16T12:33:31Z","date_created":"2023-02-24T10:45:01Z","volume":62,"external_id":{"pmid":["36738230"],"isi":["000956919900001"]},"status":"public","citation":{"ama":"Becker LM, Berbon M, Vallet A, et al. The rigid core and flexible surface of amyloid fibrils probed by Magic‐Angle Spinning NMR of aromatic residues. <i>Angewandte Chemie International Edition</i>. 2023;62(19). doi:<a href=\"https://doi.org/10.1002/anie.202219314\">10.1002/anie.202219314</a>","ista":"Becker LM, Berbon M, Vallet A, Grelard A, Morvan E, Bardiaux B, Lichtenecker R, Ernst M, Loquet A, Schanda P. 2023. The rigid core and flexible surface of amyloid fibrils probed by Magic‐Angle Spinning NMR of aromatic residues. Angewandte Chemie International Edition. 62(19), e202219314.","mla":"Becker, Lea Marie, et al. “The Rigid Core and Flexible Surface of Amyloid Fibrils Probed by Magic‐Angle Spinning NMR of Aromatic Residues.” <i>Angewandte Chemie International Edition</i>, vol. 62, no. 19, e202219314, Wiley, 2023, doi:<a href=\"https://doi.org/10.1002/anie.202219314\">10.1002/anie.202219314</a>.","apa":"Becker, L. M., Berbon, M., Vallet, A., Grelard, A., Morvan, E., Bardiaux, B., … Schanda, P. (2023). The rigid core and flexible surface of amyloid fibrils probed by Magic‐Angle Spinning NMR of aromatic residues. <i>Angewandte Chemie International Edition</i>. Wiley. <a href=\"https://doi.org/10.1002/anie.202219314\">https://doi.org/10.1002/anie.202219314</a>","ieee":"L. M. Becker <i>et al.</i>, “The rigid core and flexible surface of amyloid fibrils probed by Magic‐Angle Spinning NMR of aromatic residues,” <i>Angewandte Chemie International Edition</i>, vol. 62, no. 19. Wiley, 2023.","chicago":"Becker, Lea Marie, Mélanie Berbon, Alicia Vallet, Axelle Grelard, Estelle Morvan, Benjamin Bardiaux, Roman Lichtenecker, Matthias Ernst, Antoine Loquet, and Paul Schanda. “The Rigid Core and Flexible Surface of Amyloid Fibrils Probed by Magic‐Angle Spinning NMR of Aromatic Residues.” <i>Angewandte Chemie International Edition</i>. Wiley, 2023. <a href=\"https://doi.org/10.1002/anie.202219314\">https://doi.org/10.1002/anie.202219314</a>.","short":"L.M. Becker, M. Berbon, A. Vallet, A. Grelard, E. Morvan, B. Bardiaux, R. Lichtenecker, M. Ernst, A. Loquet, P. Schanda, Angewandte Chemie International Edition 62 (2023)."},"intvolume":"        62","related_material":{"record":[{"relation":"other","id":"14861","status":"public"},{"relation":"research_data","status":"public","id":"12497"}],"link":[{"relation":"press_release","description":"News on ISTA website","url":"https://ista.ac.at/en/news/dancing-styles-of-atoms/"}]},"has_accepted_license":"1","publication_status":"published","oa":1,"ddc":["540"],"date_published":"2023-05-01T00:00:00Z","department":[{"_id":"GradSch"},{"_id":"PaSc"}],"pmid":1,"publisher":"Wiley","user_id":"2DF688A6-F248-11E8-B48F-1D18A9856A87","tmp":{"name":"Creative Commons Attribution-NonCommercial 4.0 International (CC BY-NC 4.0)","short":"CC BY-NC (4.0)","image":"/images/cc_by_nc.png","legal_code_url":"https://creativecommons.org/licenses/by-nc/4.0/legalcode"},"article_type":"original","article_processing_charge":"Yes (via OA deal)","publication":"Angewandte Chemie International Edition","file":[{"access_level":"open_access","date_created":"2023-08-16T12:33:31Z","checksum":"7dd083ed8850faa55c34e411ed390de9","file_id":"14072","date_updated":"2023-08-16T12:33:31Z","creator":"dernst","file_size":1422445,"content_type":"application/pdf","relation":"main_file","file_name":"2023_AngewChemInt_Becker.pdf","success":1}],"day":"01","author":[{"last_name":"Becker","first_name":"Lea Marie","full_name":"Becker, Lea Marie","orcid":"0000-0002-6401-5151","id":"36336939-eb97-11eb-a6c2-c83f1214ca79"},{"full_name":"Berbon, Mélanie","last_name":"Berbon","first_name":"Mélanie"},{"first_name":"Alicia","last_name":"Vallet","full_name":"Vallet, Alicia"},{"first_name":"Axelle","last_name":"Grelard","full_name":"Grelard, Axelle"},{"full_name":"Morvan, Estelle","first_name":"Estelle","last_name":"Morvan"},{"first_name":"Benjamin","last_name":"Bardiaux","full_name":"Bardiaux, Benjamin"},{"first_name":"Roman","last_name":"Lichtenecker","full_name":"Lichtenecker, Roman"},{"last_name":"Ernst","first_name":"Matthias","full_name":"Ernst, Matthias"},{"last_name":"Loquet","first_name":"Antoine","full_name":"Loquet, Antoine"},{"last_name":"Schanda","first_name":"Paul","full_name":"Schanda, Paul","id":"7B541462-FAF6-11E9-A490-E8DFE5697425","orcid":"0000-0002-9350-7606"}],"article_number":"e202219314","title":"The rigid core and flexible surface of amyloid fibrils probed by Magic‐Angle Spinning NMR of aromatic residues","issue":"19","language":[{"iso":"eng"}],"keyword":["General Chemistry","Catalysis"],"isi":1,"publication_identifier":{"issn":["1433-7851"],"eissn":["1521-3773"]},"quality_controlled":"1","doi":"10.1002/anie.202219314"}]