{"oa_version":"Published Version","scopus_import":"1","month":"01","publication_status":"published","date_created":"2023-09-06T12:54:36Z","date_updated":"2023-11-07T11:50:29Z","issue":"10","language":[{"iso":"eng"}],"year":"2011","publication_identifier":{"issn":["0027-8424"],"eissn":["1091-6490"]},"volume":108,"page":"3952-3957","extern":"1","publication":"PNAS","author":[{"last_name":"Bachmann","full_name":"Bachmann, Annett","first_name":"Annett"},{"last_name":"Wildemann","full_name":"Wildemann, Dirk","first_name":"Dirk"},{"first_name":"Florian M","full_name":"Praetorius, Florian M","last_name":"Praetorius","id":"dfec9381-4341-11ee-8fd8-faa02bba7d62"},{"last_name":"Fischer","full_name":"Fischer, Gunter","first_name":"Gunter"},{"first_name":"Thomas","full_name":"Kiefhaber, Thomas","last_name":"Kiefhaber"}],"status":"public","_id":"14305","quality_controlled":"1","pmid":1,"article_type":"original","citation":{"chicago":"Bachmann, Annett, Dirk Wildemann, Florian M Praetorius, Gunter Fischer, and Thomas Kiefhaber. “Mapping Backbone and Side-Chain Interactions in the Transition State of a Coupled Protein Folding and Binding Reaction.” <i>PNAS</i>. Proceedings of the National Academy of Sciences, 2011. <a href=\"https://doi.org/10.1073/pnas.1012668108\">https://doi.org/10.1073/pnas.1012668108</a>.","ama":"Bachmann A, Wildemann D, Praetorius FM, Fischer G, Kiefhaber T. Mapping backbone and side-chain interactions in the transition state of a coupled protein folding and binding reaction. <i>PNAS</i>. 2011;108(10):3952-3957. doi:<a href=\"https://doi.org/10.1073/pnas.1012668108\">10.1073/pnas.1012668108</a>","ieee":"A. Bachmann, D. Wildemann, F. M. Praetorius, G. Fischer, and T. Kiefhaber, “Mapping backbone and side-chain interactions in the transition state of a coupled protein folding and binding reaction,” <i>PNAS</i>, vol. 108, no. 10. Proceedings of the National Academy of Sciences, pp. 3952–3957, 2011.","ista":"Bachmann A, Wildemann D, Praetorius FM, Fischer G, Kiefhaber T. 2011. Mapping backbone and side-chain interactions in the transition state of a coupled protein folding and binding reaction. PNAS. 108(10), 3952–3957.","mla":"Bachmann, Annett, et al. “Mapping Backbone and Side-Chain Interactions in the Transition State of a Coupled Protein Folding and Binding Reaction.” <i>PNAS</i>, vol. 108, no. 10, Proceedings of the National Academy of Sciences, 2011, pp. 3952–57, doi:<a href=\"https://doi.org/10.1073/pnas.1012668108\">10.1073/pnas.1012668108</a>.","short":"A. Bachmann, D. Wildemann, F.M. Praetorius, G. Fischer, T. Kiefhaber, PNAS 108 (2011) 3952–3957.","apa":"Bachmann, A., Wildemann, D., Praetorius, F. M., Fischer, G., &#38; Kiefhaber, T. (2011). Mapping backbone and side-chain interactions in the transition state of a coupled protein folding and binding reaction. <i>PNAS</i>. Proceedings of the National Academy of Sciences. <a href=\"https://doi.org/10.1073/pnas.1012668108\">https://doi.org/10.1073/pnas.1012668108</a>"},"doi":"10.1073/pnas.1012668108","article_processing_charge":"No","date_published":"2011-01-12T00:00:00Z","external_id":{"pmid":["21325613"]},"intvolume":"       108","title":"Mapping backbone and side-chain interactions in the transition state of a coupled protein folding and binding reaction","oa":1,"main_file_link":[{"url":"https://doi.org/10.1073/pnas.1012668108","open_access":"1"}],"day":"12","user_id":"2DF688A6-F248-11E8-B48F-1D18A9856A87","type":"journal_article","publisher":"Proceedings of the National Academy of Sciences","abstract":[{"lang":"eng","text":"Understanding the mechanism of protein folding requires a detailed knowledge of the structural properties of the barriers separating unfolded from native conformations. The S-peptide from ribonuclease S forms its α-helical structure only upon binding to the folded S-protein. We characterized the transition state for this binding-induced folding reaction at high resolution by determining the effect of site-specific backbone thioxylation and side-chain modifications on the kinetics and thermodynamics of the reaction, which allows us to monitor formation of backbone hydrogen bonds and side-chain interactions in the transition state. The experiments reveal that α-helical structure in the S-peptide is absent in the transition state of binding. Recognition between the unfolded S-peptide and the S-protein is mediated by loosely packed hydrophobic side-chain interactions in two well defined regions on the S-peptide. Close packing and helix formation occurs rapidly after binding. Introducing hydrophobic residues at positions outside the recognition region can drastically slow down association."}],"keyword":["Multidisciplinary"]}