[{"oa_version":"Published Version","publication_identifier":{"issn":["2590-1524"]},"publication_status":"published","article_processing_charge":"No","date_created":"2023-01-12T11:55:38Z","doi":"10.1016/j.yjsbx.2022.100079","external_id":{"pmid":["36578472"]},"author":[{"last_name":"Gauto","first_name":"Diego F.","full_name":"Gauto, Diego F."},{"last_name":"Lebedenko","full_name":"Lebedenko, Olga O.","first_name":"Olga O."},{"last_name":"Becker","id":"36336939-eb97-11eb-a6c2-c83f1214ca79","orcid":"0000-0002-6401-5151","full_name":"Becker, Lea Marie","first_name":"Lea Marie"},{"last_name":"Ayala","first_name":"Isabel","full_name":"Ayala, Isabel"},{"last_name":"Lichtenecker","first_name":"Roman","full_name":"Lichtenecker, Roman"},{"last_name":"Skrynnikov","full_name":"Skrynnikov, Nikolai R.","first_name":"Nikolai R."},{"last_name":"Schanda","first_name":"Paul","full_name":"Schanda, Paul","id":"7B541462-FAF6-11E9-A490-E8DFE5697425","orcid":"0000-0002-9350-7606"}],"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."}],"file_date_updated":"2023-08-16T09:36:28Z","article_number":"100079","user_id":"2DF688A6-F248-11E8-B48F-1D18A9856A87","corr_author":"1","language":[{"iso":"eng"}],"related_material":{"record":[{"relation":"dissertation_contains","status":"public","id":"22334"}]},"publication":"Journal of Structural Biology: X","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).","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>","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>.","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.","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>."},"month":"01","volume":7,"oa":1,"date_published":"2023-01-01T00:00:00Z","tmp":{"legal_code_url":"https://creativecommons.org/licenses/by-nc-nd/4.0/legalcode","short":"CC BY-NC-ND (4.0)","image":"/images/cc_by_nc_nd.png","name":"Creative Commons Attribution-NonCommercial-NoDerivatives 4.0 International (CC BY-NC-ND 4.0)"},"article_type":"original","title":"Aromatic ring flips in differently packed ubiquitin protein crystals from MAS NMR and MD","_id":"12114","publisher":"Elsevier","quality_controlled":"1","keyword":["Structural Biology"],"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","file":[{"date_updated":"2023-08-16T09:36:28Z","creator":"dernst","content_type":"application/pdf","relation":"main_file","file_name":"2023_JourStrucBiologyX_Gauto.pdf","success":1,"file_id":"14064","access_level":"open_access","date_created":"2023-08-16T09:36:28Z","checksum":"b4b1c10a31018aafe053b7d55a470e54","file_size":5132322}],"department":[{"_id":"PaSc"}],"type":"journal_article","license":"https://creativecommons.org/licenses/by-nc-nd/4.0/","status":"public","has_accepted_license":"1","scopus_import":"1","ddc":["570"],"date_updated":"2026-07-20T09:49:12Z","day":"01","fulldoi":"https://doi.org/10.1016/j.yjsbx.2022.100079","pmid":1},{"file_date_updated":"2024-01-30T12:36:39Z","article_number":"102660","external_id":{"pmid":["37536064"],"isi":["001053616200001"]},"author":[{"full_name":"Napoli, Federico","first_name":"Federico","orcid":"0000-0002-9043-136X","id":"d42e08e7-f4fc-11eb-af0a-d71e26138f1b","last_name":"Napoli"},{"id":"36336939-eb97-11eb-a6c2-c83f1214ca79","orcid":"0000-0002-6401-5151","full_name":"Becker, Lea Marie","first_name":"Lea Marie","last_name":"Becker"},{"id":"7B541462-FAF6-11E9-A490-E8DFE5697425","orcid":"0000-0002-9350-7606","first_name":"Paul","full_name":"Schanda, Paul","last_name":"Schanda"}],"abstract":[{"lang":"eng","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."}],"publication_status":"published","article_processing_charge":"Yes (via OA deal)","date_created":"2023-08-13T22:01:11Z","doi":"10.1016/j.sbi.2023.102660","publication_identifier":{"eissn":["1879-033X"],"issn":["0959-440X"]},"oa_version":"Published Version","publication":"Current Opinion in Structural Biology","intvolume":"        82","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.","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>.","short":"F. Napoli, L.M. Becker, P. Schanda, Current Opinion in Structural Biology 82 (2023).","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>","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>","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>."},"language":[{"iso":"eng"}],"isi":1,"corr_author":"1","user_id":"2DF688A6-F248-11E8-B48F-1D18A9856A87","tmp":{"name":"Creative Commons Attribution 4.0 International Public License (CC-BY 4.0)","short":"CC BY (4.0)","image":"/images/cc_by.png","legal_code_url":"https://creativecommons.org/licenses/by/4.0/legalcode"},"oa":1,"date_published":"2023-10-01T00:00:00Z","volume":82,"month":"10","publisher":"Elsevier","_id":"14036","title":"Protein dynamics detected by magic-angle spinning relaxation dispersion NMR","article_type":"original","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.","quality_controlled":"1","department":[{"_id":"PaSc"}],"year":"2023","file":[{"success":1,"checksum":"c850f7ac8a4234319755b672c1df69ae","file_id":"14907","date_created":"2024-01-30T12:36:39Z","access_level":"open_access","file_size":1231998,"date_updated":"2024-01-30T12:36:39Z","creator":"dernst","relation":"main_file","file_name":"2023_CurrentOpinionStrucBio_Napoli.pdf","content_type":"application/pdf"}],"status":"public","type":"journal_article","project":[{"grant_number":"I05812","name":"AlloSpace. The emergence and mechanisms of allostery","_id":"eb9c82eb-77a9-11ec-83b8-aadd536561cf"}],"issue":"10","date_updated":"2025-04-14T09:10:17Z","day":"01","fulldoi":"https://doi.org/10.1016/j.sbi.2023.102660","pmid":1,"ddc":["570"],"scopus_import":"1"},{"related_material":{"link":[{"url":"https://doi.org/10.1038/s41467-022-31243-1","relation":"erratum"}]},"language":[{"iso":"eng"}],"corr_author":"1","user_id":"2DF688A6-F248-11E8-B48F-1D18A9856A87","isi":1,"intvolume":"        13","citation":{"apa":"Gauto, D. F., Macek, P., Malinverni, D., Fraga, H., Paloni, M., Sučec, I., … Schanda, P. (2022). Functional control of a 0.5 MDa TET aminopeptidase by a flexible loop revealed by MAS NMR. <i>Nature Communications</i>. Springer Nature. <a href=\"https://doi.org/10.1038/s41467-022-29423-0\">https://doi.org/10.1038/s41467-022-29423-0</a>","mla":"Gauto, Diego F., et al. “Functional Control of a 0.5 MDa TET Aminopeptidase by a Flexible Loop Revealed by MAS NMR.” <i>Nature Communications</i>, vol. 13, 1927, Springer Nature, 2022, doi:<a href=\"https://doi.org/10.1038/s41467-022-29423-0\">10.1038/s41467-022-29423-0</a>.","ama":"Gauto DF, Macek P, Malinverni D, et al. Functional control of a 0.5 MDa TET aminopeptidase by a flexible loop revealed by MAS NMR. <i>Nature Communications</i>. 2022;13. doi:<a href=\"https://doi.org/10.1038/s41467-022-29423-0\">10.1038/s41467-022-29423-0</a>","short":"D.F. Gauto, P. Macek, D. Malinverni, H. Fraga, M. Paloni, I. Sučec, A. Hessel, J.P. Bustamante, A. Barducci, P. Schanda, Nature Communications 13 (2022).","ista":"Gauto DF, Macek P, Malinverni D, Fraga H, Paloni M, Sučec I, Hessel A, Bustamante JP, Barducci A, Schanda P. 2022. Functional control of a 0.5 MDa TET aminopeptidase by a flexible loop revealed by MAS NMR. Nature Communications. 13, 1927.","ieee":"D. F. Gauto <i>et al.</i>, “Functional control of a 0.5 MDa TET aminopeptidase by a flexible loop revealed by MAS NMR,” <i>Nature Communications</i>, vol. 13. Springer Nature, 2022.","chicago":"Gauto, Diego F., Pavel Macek, Duccio Malinverni, Hugo Fraga, Matteo Paloni, Iva Sučec, Audrey Hessel, Juan Pablo Bustamante, Alessandro Barducci, and Paul Schanda. “Functional Control of a 0.5 MDa TET Aminopeptidase by a Flexible Loop Revealed by MAS NMR.” <i>Nature Communications</i>. Springer Nature, 2022. <a href=\"https://doi.org/10.1038/s41467-022-29423-0\">https://doi.org/10.1038/s41467-022-29423-0</a>."},"publication":"Nature Communications","publication_status":"published","doi":"10.1038/s41467-022-29423-0","date_created":"2022-04-17T22:01:45Z","article_processing_charge":"No","publication_identifier":{"eissn":["2041-1723"]},"oa_version":"Published Version","article_number":"1927","file_date_updated":"2022-05-02T08:48:00Z","author":[{"last_name":"Gauto","full_name":"Gauto, Diego F.","first_name":"Diego F."},{"first_name":"Pavel","full_name":"Macek, Pavel","last_name":"Macek"},{"last_name":"Malinverni","first_name":"Duccio","full_name":"Malinverni, Duccio"},{"last_name":"Fraga","first_name":"Hugo","full_name":"Fraga, Hugo"},{"last_name":"Paloni","first_name":"Matteo","full_name":"Paloni, Matteo"},{"last_name":"Sučec","first_name":"Iva","full_name":"Sučec, Iva"},{"last_name":"Hessel","full_name":"Hessel, Audrey","first_name":"Audrey"},{"first_name":"Juan Pablo","full_name":"Bustamante, Juan Pablo","last_name":"Bustamante"},{"first_name":"Alessandro","full_name":"Barducci, Alessandro","last_name":"Barducci"},{"id":"7B541462-FAF6-11E9-A490-E8DFE5697425","orcid":"0000-0002-9350-7606","first_name":"Paul","full_name":"Schanda, Paul","last_name":"Schanda"}],"abstract":[{"lang":"eng","text":"Large oligomeric enzymes control a myriad of cellular processes, from protein synthesis and degradation to metabolism. The 0.5 MDa large TET2 aminopeptidase, a prototypical protease important for cellular homeostasis, degrades peptides within a ca. 60 Å wide tetrahedral chamber with four lateral openings. The mechanisms of substrate trafficking and processing remain debated. Here, we integrate magic-angle spinning (MAS) NMR, mutagenesis, co-evolution analysis and molecular dynamics simulations and reveal that a loop in the catalytic chamber is a key element for enzymatic function. The loop is able to stabilize ligands in the active site and may additionally have a direct role in activating the catalytic water molecule whereby a conserved histidine plays a key role. Our data provide a strong case for the functional importance of highly dynamic - and often overlooked - parts of an enzyme, and the potential of MAS NMR to investigate their dynamics at atomic resolution."}],"external_id":{"pmid":["35395851"],"isi":["000781498700009"]},"title":"Functional control of a 0.5 MDa TET aminopeptidase by a flexible loop revealed by MAS NMR","article_type":"original","publisher":"Springer Nature","_id":"11179","date_published":"2022-04-08T00:00:00Z","oa":1,"volume":13,"month":"04","tmp":{"name":"Creative Commons Attribution 4.0 International Public License (CC-BY 4.0)","short":"CC BY (4.0)","image":"/images/cc_by.png","legal_code_url":"https://creativecommons.org/licenses/by/4.0/legalcode"},"department":[{"_id":"PaSc"}],"file":[{"success":1,"file_id":"11348","access_level":"open_access","date_created":"2022-05-02T08:48:00Z","checksum":"db61d5534e988743d6266d3675d77b08","file_size":2637590,"date_updated":"2022-05-02T08:48:00Z","creator":"dernst","content_type":"application/pdf","relation":"main_file","file_name":"2022_NatureCommunications_Gauto.pdf"}],"year":"2022","quality_controlled":"1","acknowledgement":"We are grateful to Bernhard Brutscher, Alicia Vallet, and Adrien Favier for excellent NMR\r\nplatform operation and management. The plasmid coding for TET2 was kindly provided\r\nby Bruno Franzetti and Jerome Boisbouvier (IBS Grenoble). We thank Anne-Marie Villard\r\nand the RoBioMol platform for preparing the loop deletion construct. The RoBioMol\r\nplatform is part of the Grenoble Instruct-ERIC center (ISBG; UAR 3518 CNRS-CEAUGA-EMBL) within the Grenoble Partnership for Structural Biology (PSB), supported by FRISBI (ANR-10-INBS-0005-02) and GRAL (ANR-10-LABX-49-01), financed within the University Grenoble Alpes graduate school (Ecoles Universitaires de Recherche) CBHEUR-GS (ANR-17-EURE-0003). This work was supported by the European Research Council (StG-2012-311318-ProtDyn2Function to P. S.) and the French Agence Nationale de la Recherche (ANR), under grant ANR-14-ACHN-0016 (M.P. and A.B.).","ddc":["570"],"scopus_import":"1","fulldoi":"https://doi.org/10.1038/s41467-022-29423-0","pmid":1,"day":"08","date_updated":"2025-06-11T13:31:55Z","has_accepted_license":"1","status":"public","type":"journal_article"},{"type":"journal_article","status":"public","has_accepted_license":"1","day":"25","date_updated":"2024-10-09T21:01:12Z","pmid":1,"fulldoi":"https://doi.org/10.3389/fmolb.2021.762005","scopus_import":"1","ddc":["547"],"acknowledgement":"We thank Juan C. Fontecilla-Camps for insightful discussions related to ATP-driven machineries, and Elif Karagöz for providing the structural model of the Hsp90-Tau complex. This study was supported by the European Research Council (StG-2012-311318-ProtDyn2Function) and the Agence Nationale de la Recherche (ANR-18-CE92-0032-MitoMemProtImp).","quality_controlled":"1","year":"2021","file":[{"creator":"cchlebak","content_type":"application/pdf","file_name":"2021_FrontiersMolBioSc_Sučec.pdf","relation":"main_file","date_updated":"2021-11-23T15:06:58Z","access_level":"open_access","date_created":"2021-11-23T15:06:58Z","file_id":"10333","checksum":"a5c9dbf80dc2c5aaa737f456c941d964","file_size":4700798,"success":1}],"department":[{"_id":"PaSc"}],"tmp":{"name":"Creative Commons Attribution 4.0 International Public License (CC-BY 4.0)","short":"CC BY (4.0)","image":"/images/cc_by.png","legal_code_url":"https://creativecommons.org/licenses/by/4.0/legalcode"},"volume":8,"month":"10","oa":1,"date_published":"2021-10-25T00:00:00Z","_id":"10323","publisher":"Frontiers","article_type":"original","title":"How do chaperones bind (partly) unfolded client proteins?","external_id":{"isi":["000717241700001"],"pmid":["34760928"]},"author":[{"full_name":"Sučec, Iva","first_name":"Iva","last_name":"Sučec"},{"first_name":"Beate","full_name":"Bersch, Beate","last_name":"Bersch"},{"last_name":"Schanda","full_name":"Schanda, Paul","first_name":"Paul","orcid":"0000-0002-9350-7606","id":"7B541462-FAF6-11E9-A490-E8DFE5697425"}],"abstract":[{"lang":"eng","text":"Molecular chaperones are central to cellular protein homeostasis. Dynamic disorder is a key feature of the complexes of molecular chaperones and their client proteins, and it facilitates the client release towards a folded state or the handover to downstream components. The dynamic nature also implies that a given chaperone can interact with many different client proteins, based on physico-chemical sequence properties rather than on structural complementarity of their (folded) 3D structure. Yet, the balance between this promiscuity and some degree of client specificity is poorly understood. Here, we review recent atomic-level descriptions of chaperones with client proteins, including chaperones in complex with intrinsically disordered proteins, with membrane-protein precursors, or partially folded client proteins. We focus hereby on chaperone-client interactions that are independent of ATP. The picture emerging from these studies highlights the importance of dynamics in these complexes, whereby several interaction types, not only hydrophobic ones, contribute to the complex formation. We discuss these features of chaperone-client complexes and possible factors that may contribute to this balance of promiscuity and specificity."}],"file_date_updated":"2021-11-23T15:06:58Z","article_number":"762005","oa_version":"Published Version","publication_identifier":{"eissn":["2296-889X"]},"article_processing_charge":"Yes (via OA deal)","doi":"10.3389/fmolb.2021.762005","publication_status":"published","date_created":"2021-11-21T23:01:29Z","publication":"Frontiers in Molecular Biosciences","intvolume":"         8","citation":{"ista":"Sučec I, Bersch B, Schanda P. 2021. How do chaperones bind (partly) unfolded client proteins? Frontiers in Molecular Biosciences. 8, 762005.","ieee":"I. Sučec, B. Bersch, and P. Schanda, “How do chaperones bind (partly) unfolded client proteins?,” <i>Frontiers in Molecular Biosciences</i>, vol. 8. Frontiers, 2021.","chicago":"Sučec, Iva, Beate Bersch, and Paul Schanda. “How Do Chaperones Bind (Partly) Unfolded Client Proteins?” <i>Frontiers in Molecular Biosciences</i>. Frontiers, 2021. <a href=\"https://doi.org/10.3389/fmolb.2021.762005\">https://doi.org/10.3389/fmolb.2021.762005</a>.","ama":"Sučec I, Bersch B, Schanda P. How do chaperones bind (partly) unfolded client proteins? <i>Frontiers in Molecular Biosciences</i>. 2021;8. doi:<a href=\"https://doi.org/10.3389/fmolb.2021.762005\">10.3389/fmolb.2021.762005</a>","short":"I. Sučec, B. Bersch, P. Schanda, Frontiers in Molecular Biosciences 8 (2021).","mla":"Sučec, Iva, et al. “How Do Chaperones Bind (Partly) Unfolded Client Proteins?” <i>Frontiers in Molecular Biosciences</i>, vol. 8, 762005, Frontiers, 2021, doi:<a href=\"https://doi.org/10.3389/fmolb.2021.762005\">10.3389/fmolb.2021.762005</a>.","apa":"Sučec, I., Bersch, B., &#38; Schanda, P. (2021). How do chaperones bind (partly) unfolded client proteins? <i>Frontiers in Molecular Biosciences</i>. Frontiers. <a href=\"https://doi.org/10.3389/fmolb.2021.762005\">https://doi.org/10.3389/fmolb.2021.762005</a>"},"isi":1,"corr_author":"1","user_id":"4359f0d1-fa6c-11eb-b949-802e58b17ae8","language":[{"iso":"eng"}]}]