[{"department":[{"_id":"PaSc"}],"date_created":"2024-01-22T08:04:57Z","article_processing_charge":"No","publication_status":"published","intvolume":"        29","alternative_title":["New Developments in NMR"],"title":"Preparing Chaperone–Client Protein Complexes for Biophysical and Structural Studies","_id":"14847","author":[{"first_name":"I.","last_name":"Sučec","full_name":"Sučec, I."},{"id":"7B541462-FAF6-11E9-A490-E8DFE5697425","last_name":"Schanda","first_name":"Paul","full_name":"Schanda, Paul","orcid":"0000-0002-9350-7606"}],"editor":[{"full_name":"Hiller, Sebastian","first_name":"Sebastian","last_name":"Hiller"},{"full_name":"Liu, Maili","first_name":"Maili","last_name":"Liu"},{"last_name":"He","first_name":"Lichun","full_name":"He, Lichun"}],"publisher":"Royal Society of Chemistry","quality_controlled":"1","page":"136-161","day":"01","doi":"10.1039/bk9781839165986-00136","abstract":[{"lang":"eng","text":"Understanding the mechanisms of chaperones at the atomic level generally requires producing chaperone–client complexes in vitro. This task comes with significant challenges, because one needs to find conditions in which the client protein is presented to the chaperone in a state that binds and at the same time avoid the pitfalls of protein aggregation that are often inherent to such states. The strategy differs significantly for different client proteins and chaperones, but there are common underlying principles. Here, we discuss these principles and deduce the strategies that can be successfully applied for different chaperone–client complexes. We review successful biochemical strategies applied to making the client protein “binding competent” and illustrate the different strategies with examples of recent biophysical and biochemical studies."}],"citation":{"mla":"Sučec, I., and Paul Schanda. “Preparing Chaperone–Client Protein Complexes for Biophysical and Structural Studies.” <i>Biophysics of Molecular Chaperones</i>, edited by Sebastian Hiller et al., vol. 29, Royal Society of Chemistry, 2023, pp. 136–61, doi:<a href=\"https://doi.org/10.1039/bk9781839165986-00136\">10.1039/bk9781839165986-00136</a>.","short":"I. Sučec, P. Schanda, in:, S. Hiller, M. Liu, L. He (Eds.), Biophysics of Molecular Chaperones, Royal Society of Chemistry, 2023, pp. 136–161.","ista":"Sučec I, Schanda P. 2023.Preparing Chaperone–Client Protein Complexes for Biophysical and Structural Studies. In: Biophysics of Molecular Chaperones. New Developments in NMR, vol. 29, 136–161.","apa":"Sučec, I., &#38; Schanda, P. (2023). Preparing Chaperone–Client Protein Complexes for Biophysical and Structural Studies. In S. Hiller, M. Liu, &#38; L. He (Eds.), <i>Biophysics of Molecular Chaperones</i> (Vol. 29, pp. 136–161). Royal Society of Chemistry. <a href=\"https://doi.org/10.1039/bk9781839165986-00136\">https://doi.org/10.1039/bk9781839165986-00136</a>","ama":"Sučec I, Schanda P. Preparing Chaperone–Client Protein Complexes for Biophysical and Structural Studies. In: Hiller S, Liu M, He L, eds. <i>Biophysics of Molecular Chaperones</i>. Vol 29. Royal Society of Chemistry; 2023:136-161. doi:<a href=\"https://doi.org/10.1039/bk9781839165986-00136\">10.1039/bk9781839165986-00136</a>","ieee":"I. Sučec and P. Schanda, “Preparing Chaperone–Client Protein Complexes for Biophysical and Structural Studies,” in <i>Biophysics of Molecular Chaperones</i>, vol. 29, S. Hiller, M. Liu, and L. He, Eds. Royal Society of Chemistry, 2023, pp. 136–161.","chicago":"Sučec, I., and Paul Schanda. “Preparing Chaperone–Client Protein Complexes for Biophysical and Structural Studies.” In <i>Biophysics of Molecular Chaperones</i>, edited by Sebastian Hiller, Maili Liu, and Lichun He, 29:136–61. Royal Society of Chemistry, 2023. <a href=\"https://doi.org/10.1039/bk9781839165986-00136\">https://doi.org/10.1039/bk9781839165986-00136</a>."},"year":"2023","date_updated":"2024-01-23T11:50:10Z","volume":29,"oa_version":"Preprint","month":"11","publication":"Biophysics of Molecular Chaperones","language":[{"iso":"eng"}],"publication_identifier":{"isbn":["9781839162824"],"eisbn":["9781839165993"]},"oa":1,"type":"book_chapter","date_published":"2023-11-01T00:00:00Z","main_file_link":[{"url":"https://doi.org/10.26434/chemrxiv-2023-rpn28","open_access":"1"}],"status":"public","user_id":"2DF688A6-F248-11E8-B48F-1D18A9856A87"},{"user_id":"2DF688A6-F248-11E8-B48F-1D18A9856A87","status":"public","volume":29,"type":"book_chapter","date_published":"2023-11-01T00:00:00Z","citation":{"ama":"Wruck F, Avellaneda Sarrió M, Naqvi MM, et al. Probing Single Chaperone Substrates. In: Hiller S, Liu M, He L, eds. <i>Biophysics of Molecular Chaperones</i>. Vol 29. Royal Society of Chemistry; 2023:278-318. doi:<a href=\"https://doi.org/10.1039/bk9781839165986-00278\">10.1039/bk9781839165986-00278</a>","apa":"Wruck, F., Avellaneda Sarrió, M., Naqvi, M. M., Koers, E. J., Till, K., Gross, L., … Tans, S. J. (2023). Probing Single Chaperone Substrates. In S. Hiller, M. Liu, &#38; L. He (Eds.), <i>Biophysics of Molecular Chaperones</i> (Vol. 29, pp. 278–318). Royal Society of Chemistry. <a href=\"https://doi.org/10.1039/bk9781839165986-00278\">https://doi.org/10.1039/bk9781839165986-00278</a>","chicago":"Wruck, F., Mario Avellaneda Sarrió, M. M. Naqvi, E. J. Koers, K. Till, L. Gross, F. Moayed, et al. “Probing Single Chaperone Substrates.” In <i>Biophysics of Molecular Chaperones</i>, edited by Sebastian Hiller, Maili Liu, and Lichun He, 29:278–318. Royal Society of Chemistry, 2023. <a href=\"https://doi.org/10.1039/bk9781839165986-00278\">https://doi.org/10.1039/bk9781839165986-00278</a>.","ieee":"F. Wruck <i>et al.</i>, “Probing Single Chaperone Substrates,” in <i>Biophysics of Molecular Chaperones</i>, vol. 29, S. Hiller, M. Liu, and L. He, Eds. Royal Society of Chemistry, 2023, pp. 278–318.","short":"F. Wruck, M. Avellaneda Sarrió, M.M. Naqvi, E.J. Koers, K. Till, L. Gross, F. Moayed, A. Roland, L.W.H.J. Heling, A. Mashaghi, S.J. Tans, in:, S. Hiller, M. Liu, L. He (Eds.), Biophysics of Molecular Chaperones, Royal Society of Chemistry, 2023, pp. 278–318.","mla":"Wruck, F., et al. “Probing Single Chaperone Substrates.” <i>Biophysics of Molecular Chaperones</i>, edited by Sebastian Hiller et al., vol. 29, Royal Society of Chemistry, 2023, pp. 278–318, doi:<a href=\"https://doi.org/10.1039/bk9781839165986-00278\">10.1039/bk9781839165986-00278</a>.","ista":"Wruck F, Avellaneda Sarrió M, Naqvi MM, Koers EJ, Till K, Gross L, Moayed F, Roland A, Heling LWHJ, Mashaghi A, Tans SJ. 2023.Probing Single Chaperone Substrates. In: Biophysics of Molecular Chaperones. New Developments in NMR, vol. 29, 278–318."},"year":"2023","date_updated":"2024-01-23T12:01:53Z","abstract":[{"text":"Regulating protein states is considered the core function of chaperones. However, despite their importance to all major cellular processes, the conformational changes that chaperones impart on polypeptide chains are difficult to study directly due to their heterogeneous, dynamic, and multi-step nature. Here, we review recent advances towards this aim using single-molecule manipulation methods, which are rapidly revealing new mechanisms of conformational control and helping to define a different perspective on the chaperone function.","lang":"eng"}],"publication_identifier":{"isbn":["9781839162824"],"eisbn":["9781839165993"]},"day":"01","doi":"10.1039/bk9781839165986-00278","language":[{"iso":"eng"}],"quality_controlled":"1","page":"278-318","editor":[{"first_name":"Sebastian","last_name":"Hiller","full_name":"Hiller, Sebastian"},{"full_name":"Liu, Maili","first_name":"Maili","last_name":"Liu"},{"last_name":"He","first_name":"Lichun","full_name":"He, Lichun"}],"publisher":"Royal Society of Chemistry","author":[{"last_name":"Wruck","first_name":"F.","full_name":"Wruck, F."},{"first_name":"Mario","last_name":"Avellaneda Sarrió","orcid":"0000-0001-6406-524X","full_name":"Avellaneda Sarrió, Mario","id":"DC4BA84C-56E6-11EA-AD5D-348C3DDC885E"},{"last_name":"Naqvi","first_name":"M. M.","full_name":"Naqvi, M. M."},{"last_name":"Koers","first_name":"E. J.","full_name":"Koers, E. J."},{"first_name":"K.","last_name":"Till","full_name":"Till, K."},{"first_name":"L.","last_name":"Gross","full_name":"Gross, L."},{"first_name":"F.","last_name":"Moayed","full_name":"Moayed, F."},{"full_name":"Roland, A.","last_name":"Roland","first_name":"A."},{"last_name":"Heling","first_name":"L. W. H. J.","full_name":"Heling, L. W. H. J."},{"first_name":"A.","last_name":"Mashaghi","full_name":"Mashaghi, A."},{"last_name":"Tans","first_name":"S. J.","full_name":"Tans, S. J."}],"publication":"Biophysics of Molecular Chaperones","_id":"14848","intvolume":"        29","alternative_title":["New Developments in NMR"],"month":"11","title":"Probing Single Chaperone Substrates","date_created":"2024-01-22T08:07:02Z","department":[{"_id":"MiSi"}],"article_processing_charge":"No","oa_version":"None","publication_status":"published"}]