{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"institution":[{"name":"bioRxiv"}],"indexed":{"date-parts":[[2026,8,30]],"date-time":"2026-08-30T02:50:51Z","timestamp":1788058251294,"version":"build-2784847793"},"posted":{"date-parts":[[2026,7,31]]},"group-title":"Biochemistry","reference-count":60,"publisher":"openRxiv","license":[{"start":{"date-parts":[[2026,7,31]],"date-time":"2026-07-31T00:00:00Z","timestamp":1785456000000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"funder":[{"award":["CHE-2203909"],"award-info":[{"award-number":["CHE-2203909"]}],"id":[{"id":"https:\/\/ror.org\/021nxhr62","id-type":"ROR","asserted-by":"publisher"}]},{"DOI":"10.13039\/100000002","name":"National Institutes of Health","doi-asserted-by":"crossref","award":["R01-GM49758"],"award-info":[{"award-number":["R01-GM49758"]}],"id":[{"id":"10.13039\/100000002","id-type":"DOI","asserted-by":"crossref"}]},{"DOI":"10.13039\/100000002","name":"National Institutes of Health","doi-asserted-by":"crossref","award":["R35-GM163533"],"award-info":[{"award-number":["R35-GM163533"]}],"id":[{"id":"10.13039\/100000002","id-type":"DOI","asserted-by":"crossref"}]},{"DOI":"10.13039\/100000002","name":"National Institutes of Health","doi-asserted-by":"crossref","award":["T32-GM008275"],"award-info":[{"award-number":["T32-GM008275"]}],"id":[{"id":"10.13039\/100000002","id-type":"DOI","asserted-by":"crossref"}]},{"DOI":"10.13039\/100000002","name":"National Institutes of Health","doi-asserted-by":"crossref","award":["T32-GM133398"],"award-info":[{"award-number":["T32-GM133398"]}],"id":[{"id":"10.13039\/100000002","id-type":"DOI","asserted-by":"crossref"}]},{"DOI":"10.13039\/100000002","name":"National Institutes of Health","doi-asserted-by":"crossref","award":["R01-GM118510"],"award-info":[{"award-number":["R01-GM118510"]}],"id":[{"id":"10.13039\/100000002","id-type":"DOI","asserted-by":"crossref"}]},{"DOI":"10.13039\/100000002","name":"National Institutes of Health","doi-asserted-by":"crossref","award":["R01-GM087605"],"award-info":[{"award-number":["R01-GM087605"]}],"id":[{"id":"10.13039\/100000002","id-type":"DOI","asserted-by":"crossref"}]}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":[],"accepted":{"date-parts":[[2026,7,31]]},"abstract":"<jats:title>Abstract<\/jats:title>\n                <jats:p>Thioamides are natural post-translational modifications of the peptide backbone and can be introduced synthetically to probe protein folding or functionalize peptides for translational applications. In this work, we demonstrate that thioamide-containing peptides with C-terminal thioesters can be efficiently generated using Knorr pyrazole activation and used in subsequent native chemical ligation reactions to generate thioamide containing proteins. We compare this method to acyl azide activation and find that both routes provide similar yields. We also investigate ultrasound-mediated desulfurization of the ligation site cysteine for potential advantages over chemical radical initiators. Scaling up our syntheses allows us to study thioamide perturbations to the \u03b2-sheet region of the B1 domain of protein G (GB1) as well as \u03b2-strand interactions in amyloid fibrils of the Parkinson\u2019s disease protein \u03b1-synuclein. In both contexts, we observe dramatic destabilization of the \u03b2-sheet networks, manifested in decreased GB1 thermal stability and altered folding and slowed aggregation of \u03b1-synuclein. These findings illustrate the impact that a single atom substitution can have on cooperative hydrogen bonding networks and prompt future study of both systems.<\/jats:p>","DOI":"10.64898\/2026.07.30.741859","type":"posted-content","created":{"date-parts":[[2026,7,31]],"date-time":"2026-07-31T14:45:14Z","timestamp":1785509114000},"source":"Crossref","is-referenced-by-count":1,"title":["Improved Protein Semi-Synthesis Enables Biophysical Studies of Thioamide Destabilization of \u03b2-Sheet Interactions"],"prefix":"10.64898","author":[{"ORCID":"https:\/\/orcid.org\/0009-0002-3621-5081","authenticated-orcid":false,"given":"Evan S. K.","family":"Yanagawa","sequence":"first","affiliation":[{"name":"Department of Chemistry, School of Arts and Sciences, University of Pennsylvania; 231 S. 34th Street, Philadelphia, PA 19104, USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-8527-5657","authenticated-orcid":false,"given":"Kristen E.","family":"Fiore","sequence":"additional","affiliation":[{"name":"Department of Chemistry, School of Arts and Sciences, University of Pennsylvania; 231 S. 34th Street, Philadelphia, PA 19104, USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Denver Y.","family":"Francis","sequence":"additional","affiliation":[{"name":"Department of Chemistry, School of Arts and Sciences, University of Pennsylvania; 231 S. 34th Street, Philadelphia, PA 19104, USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Aiden","family":"Lesneski","sequence":"additional","affiliation":[{"name":"Department of Chemistry, School of Arts and Sciences, University of Pennsylvania; 231 S. 34th Street, Philadelphia, PA 19104, USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0009-0003-1862-6220","authenticated-orcid":false,"given":"Yanan","family":"Chang","sequence":"additional","affiliation":[{"name":"Department of Chemistry, School of Arts and Sciences, University of Pennsylvania; 231 S. 34th Street, Philadelphia, PA 19104, USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0003-3333-5053","authenticated-orcid":false,"given":"Benjamin","family":"Roose","sequence":"additional","affiliation":[{"name":"Department of Chemistry, School of Arts and Sciences, University of Pennsylvania; 231 S. 34th Street, Philadelphia, PA 19104, USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-0194-5212","authenticated-orcid":false,"given":"David","family":"Christianson","sequence":"additional","affiliation":[{"name":"Department of Chemistry, School of Arts and Sciences, University of Pennsylvania; 231 S. 34th Street, Philadelphia, PA 19104, USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0001-6877-9223","authenticated-orcid":false,"given":"Kohei","family":"Sato","sequence":"additional","affiliation":[{"name":"Department of Engineering, Graduate School of Integrated Science and Technology, Shizuoka University, 3-5-1 Johoku, Hamamatsu, Shizuoka 432-8561, Japan"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0003-3854-9210","authenticated-orcid":false,"given":"E. James","family":"Petersson","sequence":"additional","affiliation":[{"name":"Department of Chemistry, School of Arts and Sciences, University of Pennsylvania; 231 S. 34th Street, Philadelphia, PA 19104, USA"},{"name":"Department of Biochemistry and Biophysics, Perelman School of Medicine, University of Pennsylvania, 421 Curie Boulevard, Philadelphia, PA 19104, USA"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"54368","reference":[{"issue":"1","key":"2026080406301722000_2026.07.30.741859v1.1","doi-asserted-by":"crossref","first-page":"117","DOI":"10.1021\/bi00270a017","article-title":"Transition-state stabilization at the oxyanion binding sites of serine and thiol proteinases: hydrolyses of thiono and oxygen esters","volume":"22","year":"1983","journal-title":"Biochemistry"},{"issue":"2","key":"2026080406301722000_2026.07.30.741859v1.2","doi-asserted-by":"crossref","first-page":"142","DOI":"10.1021\/acschembio.8b01022","article-title":"Biosynthesis and Chemical Applications of Thioamides","volume":"14","year":"2019","journal-title":"ACS Chemical Biology"},{"issue":"11","key":"2026080406301722000_2026.07.30.741859v1.3","doi-asserted-by":"crossref","first-page":"1320","DOI":"10.1021\/acs.accounts.2c00701","article-title":"Urea- and Thiourea-Based Receptors for Anion Binding","volume":"56","year":"2023","journal-title":"Accounts of Chemical Research"},{"issue":"2","key":"2026080406301722000_2026.07.30.741859v1.4","doi-asserted-by":"crossref","first-page":"381","DOI":"10.1111\/j.1432-1033.1997.00381.x","article-title":"Probing Substrate Backbone Function in Prolyl Oligopeptidase Catalysis","volume":"245","year":"1997","journal-title":"European Journal of Biochemistry"},{"key":"2026080406301722000_2026.07.30.741859v1.5","doi-asserted-by":"publisher","DOI":"10.1021\/bi00536a022"},{"key":"2026080406301722000_2026.07.30.741859v1.6","doi-asserted-by":"publisher","DOI":"10.1042\/bj2450285"},{"key":"2026080406301722000_2026.07.30.741859v1.7","doi-asserted-by":"publisher","DOI":"10.1016\/0162-0134(86)80074-5"},{"key":"2026080406301722000_2026.07.30.741859v1.8","doi-asserted-by":"publisher","DOI":"10.1021\/cr950066q"},{"issue":"30","key":"2026080406301722000_2026.07.30.741859v1.9","doi-asserted-by":"crossref","first-page":"5981","DOI":"10.1039\/D2OB00412G","article-title":"Transamidation of thioamides with nucleophilic amines: thioamide N\u2013C(S) activation by ground-state-destabilization","volume":"20","year":"2022","journal-title":"Organic & Biomolecular Chemistry"},{"key":"2026080406301722000_2026.07.30.741859v1.10","first-page":"997","article-title":"207","volume":"0","year":"1960","journal-title":"An accurate determination of the crystal structure of thioacetamide. Journal of the Chemical Society (Resumed"},{"issue":"30","key":"2026080406301722000_2026.07.30.741859v1.11","doi-asserted-by":"crossref","first-page":"7010","DOI":"10.1021\/jp025516e","article-title":"Hydrogen Bonding Abilities of Thioamide","volume":"106","year":"2002","journal-title":"The Journal of Physical Chemistry A"},{"issue":"3","key":"2026080406301722000_2026.07.30.741859v1.12","doi-asserted-by":"crossref","first-page":"823","DOI":"10.1021\/jo01278a074","article-title":"Proton magnetic resonance spectra of thiocarboxamides","volume":"32","year":"1967","journal-title":"The Journal of Organic Chemistry"},{"key":"2026080406301722000_2026.07.30.741859v1.13","doi-asserted-by":"publisher","DOI":"10.1021\/ar00156a004"},{"issue":"46","key":"2026080406301722000_2026.07.30.741859v1.14","doi-asserted-by":"crossref","first-page":"16688","DOI":"10.1021\/jacs.7b08417","article-title":"Thioamide Substitution Selectively Modulates Proteolysis and Receptor Activity of Therapeutic Peptide Hormones","volume":"139","year":"2017","journal-title":"Journal of the American Chemical Society"},{"issue":"3","key":"2026080406301722000_2026.07.30.741859v1.15","doi-asserted-by":"crossref","first-page":"774","DOI":"10.1021\/acschembio.9b01036","article-title":"Studies of Thioamide Effects on Serine Protease Activity Enable Two-Site Stabilization of Cancer Imaging Peptides","volume":"15","year":"2020","journal-title":"ACS Chem Biol"},{"issue":"3","key":"2026080406301722000_2026.07.30.741859v1.16","doi-asserted-by":"crossref","first-page":"447","DOI":"10.1016\/0304-4165(94)90075-2","article-title":"Peptidyl thioamides as substrates and inhibitors of papain, and as probes of the kinetic significance of the oxyanion hole","volume":"1201","year":"1994","journal-title":"Biochimica et Biophysica Acta (BBA) - General Subjects"},{"key":"2026080406301722000_2026.07.30.741859v1.17","doi-asserted-by":"publisher","DOI":"10.7554\/eLife.60482"},{"key":"2026080406301722000_2026.07.30.741859v1.18","doi-asserted-by":"publisher","DOI":"10.1006\/jmbi.2000.4136"},{"issue":"15","key":"2026080406301722000_2026.07.30.741859v1.19","doi-asserted-by":"crossref","first-page":"6827","DOI":"10.1039\/C3CP55525A","article-title":"On the use of thioamides as fluorescence quenching probes for tracking protein folding and stability","volume":"16","year":"2014","journal-title":"Physical Chemistry Chemical Physics"},{"issue":"89","key":"2026080406301722000_2026.07.30.741859v1.20","doi-asserted-by":"crossref","first-page":"13075","DOI":"10.1039\/D4CC03309D","article-title":"Thioamide-based fluorescent sensors for dipeptidyl peptidase 4","volume":"60","year":"2024","journal-title":"Chemical Communications"},{"issue":"12","key":"2026080406301722000_2026.07.30.741859v1.21","doi-asserted-by":"crossref","first-page":"1913","DOI":"10.1021\/acs.bioconjchem.4c00411","article-title":"Improved Large-Scale Synthesis of Acridonylalanine for Diverse Peptide and Protein Applications","volume":"35","year":"2024","journal-title":"Bioconjugate Chemistry"},{"issue":"42","key":"2026080406301722000_2026.07.30.741859v1.22","doi-asserted-by":"crossref","first-page":"14718","DOI":"10.1021\/ja1044924","article-title":"Thioamides as Fluorescence Quenching Probes: Minimalist Chromophores To Monitor Protein Dynamics","volume":"132","year":"2010","journal-title":"Journal of the American Chemical Society"},{"issue":"10","key":"2026080406301722000_2026.07.30.741859v1.23","doi-asserted-by":"crossref","first-page":"1550","DOI":"10.1039\/C1CC14708K","article-title":"Thioamide quenching of intrinsic protein fluorescence","volume":"48","year":"2012","journal-title":"Chemical Communications"},{"key":"2026080406301722000_2026.07.30.741859v1.24","doi-asserted-by":"publisher","DOI":"10.1021\/ja3005094"},{"issue":"50","key":"2026080406301722000_2026.07.30.741859v1.25","doi-asserted-by":"crossref","first-page":"7798","DOI":"10.1039\/C6CC00105J","article-title":"Electronic interactions of i, i + 1 dithioamides: increased fluorescence quenching and evidence for n-to-\u03c0* interactions","volume":"52","year":"2016","journal-title":"Chemical Communications"},{"issue":"22","key":"2026080406301722000_2026.07.30.741859v1.26","doi-asserted-by":"crossref","first-page":"9172","DOI":"10.1021\/ja2113245","article-title":"Native Chemical Ligation of Thioamide-Containing Peptides: Development and Application to the Synthesis of Labeled \u03b1-Synuclein for Misfolding Studies","volume":"134","year":"2012","journal-title":"Journal of the American Chemical Society"},{"issue":"17","key":"2026080406301722000_2026.07.30.741859v1.27","doi-asserted-by":"crossref","first-page":"6529","DOI":"10.1021\/ja4005943","article-title":"Labeling proteins with fluorophore\/thioamide F\u00f6rster resonant energy transfer pairs by combining unnatural amino acid mutagenesis and native chemical ligation","volume":"135","year":"2013","journal-title":"J. Am. Chem. Soc"},{"issue":"1","key":"2026080406301722000_2026.07.30.741859v1.28","doi-asserted-by":"crossref","first-page":"83","DOI":"10.1186\/s13024-021-00501-z","article-title":"Neuropathology and molecular diagnosis of Synucleinopathies","volume":"16","year":"2021","journal-title":"Molecular Neurodegeneration"},{"issue":"5","key":"2026080406301722000_2026.07.30.741859v1.29","doi-asserted-by":"crossref","first-page":"582","DOI":"10.1039\/D1CB00229E","article-title":"Structural impact of thioamide incorporation into a \u03b2-hairpin","volume":"3","year":"2022","journal-title":"RSC Chem Biol"},{"issue":"4","key":"2026080406301722000_2026.07.30.741859v1.30","doi-asserted-by":"crossref","first-page":"2868","DOI":"10.1039\/C6SC05580J","article-title":"The effects of thioamide backbone substitution on protein stability: a study in \u03b1-helical, \u03b2-sheet, and polyproline II helical contexts","volume":"8","year":"2017","journal-title":"Chem Sci"},{"issue":"18","key":"2026080406301722000_2026.07.30.741859v1.31","doi-asserted-by":"crossref","first-page":"2454","DOI":"10.1055\/s-0033-1339853","article-title":"Efficient, Traceless Semi-Synthesis of \u03b1-Synuclein Labeled with a Fluoro-phore\/Thioamide FRET Pair","volume":"24","year":"2013","journal-title":"Synlett"},{"issue":"49","key":"2026080406301722000_2026.07.30.741859v1.32","doi-asserted-by":"crossref","first-page":"18651","DOI":"10.1021\/ja409709x","article-title":"Thioamide Quenching of Fluorescent Probes through Photoinduced Electron Transfer: Mechanistic Studies and Applications","volume":"135","year":"2013","journal-title":"Journal of the American Chemical Society"},{"key":"2026080406301722000_2026.07.30.741859v1.33","doi-asserted-by":"publisher","DOI":"10.1038\/nsb0698-470"},{"issue":"12","key":"2026080406301722000_2026.07.30.741859v1.34","doi-asserted-by":"crossref","first-page":"2773","DOI":"10.1110\/ps.8.12.2773","article-title":"Synthesis, folding, and structure of the \u03b2-turn mimic modified B1 domain of streptococcal protein G","volume":"8","year":"1999","journal-title":"Protein Science"},{"issue":"8","key":"2026080406301722000_2026.07.30.741859v1.35","doi-asserted-by":"crossref","first-page":"512","DOI":"10.1038\/nnano.2008.168","article-title":"Engineered elastomeric proteins with dual elasticity can be controlled by a molecular regulator","volume":"3","year":"2008","journal-title":"Nature Nanotechnology"},{"issue":"8","key":"2026080406301722000_2026.07.30.741859v1.36","doi-asserted-by":"crossref","first-page":"3325","DOI":"10.1039\/C4SC01094A","article-title":"Folding Thermodynamics of Protein-Like Oligomers with Heterogeneous Backbones","volume":"5","year":"2014","journal-title":"Chem Sci"},{"issue":"51","key":"2026080406301722000_2026.07.30.741859v1.37","doi-asserted-by":"crossref","first-page":"14362","DOI":"10.1021\/jp075531p","article-title":"Crystal Polymorphism of Protein GB1 Examined by Solid-State NMR Spectroscopy and X-ray Diffraction","volume":"111","year":"2007","journal-title":"The Journal of Physical Chemistry B"},{"key":"2026080406301722000_2026.07.30.741859v1.38","doi-asserted-by":"publisher","DOI":"10.1016\/j.tet.2009.03.008"},{"key":"2026080406301722000_2026.07.30.741859v1.39","doi-asserted-by":"publisher","DOI":"10.1002\/anie.200705471"},{"issue":"2","key":"2026080406301722000_2026.07.30.741859v1.40","doi-asserted-by":"crossref","first-page":"87","DOI":"10.1002\/psc.2589","article-title":"Synthesis of thioester peptides for the incorporation of thioamides into proteins by native chemical ligation","volume":"20","year":"2014","journal-title":"J. Pept. Sci"},{"key":"2026080406301722000_2026.07.30.741859v1.41","doi-asserted-by":"crossref","unstructured":"Fiore, K. E. ; Phan, H. A. T. ; Robkis, D. M. ; Walters, C. R. ; Petersson, E. J. , Chapter Ten - Incorporating thioamides into proteins by native chemical ligation. In Methods in Enzymology, Petersson, E. J. , Ed. Academic Press: 2021; Vol. 656, pp 295\u2013339.","DOI":"10.1016\/bs.mie.2021.04.011"},{"issue":"26","key":"2026080406301722000_2026.07.30.741859v1.42","doi-asserted-by":"crossref","first-page":"6262","DOI":"10.1039\/C6OB01020B","article-title":"Chemoselective modifications for the traceless ligation of thioamide-containing peptides and proteins","volume":"14","year":"2016","journal-title":"Org Biomol Chem"},{"issue":"12","key":"2026080406301722000_2026.07.30.741859v1.43","doi-asserted-by":"crossref","first-page":"2483","DOI":"10.1038\/nprot.2013.152","article-title":"Chemical synthesis of proteins using peptide hydrazides as thioester surrogates","volume":"8","year":"2013","journal-title":"Nature Protocols"},{"issue":"2","key":"2026080406301722000_2026.07.30.741859v1.44","doi-asserted-by":"crossref","first-page":"169","DOI":"10.1080\/03086648608083091","article-title":"THIONO COMPOUNDS, 7. OXIDATION OF THIOAMIDES IN RELATION TO ADVERSE BIOLOGICAL EFFECTS1","volume":"26","year":"1986","journal-title":"Phosphorus and Sulfur and the Related Elements"},{"issue":"5","key":"2026080406301722000_2026.07.30.741859v1.45","doi-asserted-by":"crossref","first-page":"4135","DOI":"10.1021\/jacs.4c13464","article-title":"Mechanically Triggered Protein Desulfurization","volume":"147","year":"2025","journal-title":"Journal of the American Chemical Society"},{"issue":"50","key":"2026080406301722000_2026.07.30.741859v1.46","doi-asserted-by":"crossref","first-page":"e202414324","DOI":"10.1002\/anie.202414324","article-title":"Homonuclear Super-Resolution NMR Spectroscopy","volume":"63","year":"2024","journal-title":"Angewandte Chemie International Edition"},{"key":"2026080406301722000_2026.07.30.741859v1.47","doi-asserted-by":"crossref","unstructured":"Shimogawa, M. ; Li, M.-H. ; Park, G. S. H. ; Ramirez, J. ; Lee, H. ; Watson, P. R. ; Sharma, S. ; Lin, Z. ; Peng, C. ; Lee, V. M. Y. ; Garcia, B. A. ; Christianson, D. W. ; Rhoades, E. ; Eliezer, D. ; Petersson, E. J ., Investigation of All Disease-Relevant Lysine Acetylation Sites in \u03b1-Synuclein Enabled by Non-canonical Amino Acid Mutagenesis. eLife Sciences Publications, Ltd: 2025.","DOI":"10.7554\/eLife.109043.1"},{"key":"2026080406301722000_2026.07.30.741859v1.48","doi-asserted-by":"crossref","unstructured":"Sanchez, J. C. ; Perez, R. M. ; Guarino, D. S. ; Dhavala, D. ; Baumgardt, J. K. ; Shaffer, K. D. ; Kotzbauer, P. ; Mach, R. H. ; Petersson, E. J. ; Wright, E. R. , Complementary Structural and Chemical Biology Methods Reveal the Basis for Selective Radioligand Binding to \u03b1-Synuclein in MSA Tissue. bioRxiv 2025, 2025.06.30.662461.","DOI":"10.1101\/2025.06.30.662461"},{"key":"2026080406301722000_2026.07.30.741859v1.49","doi-asserted-by":"publisher","DOI":"10.1038\/s41422-018-0075-x"},{"key":"2026080406301722000_2026.07.30.741859v1.50","doi-asserted-by":"publisher","DOI":"10.7554\/eLife.48907"},{"key":"2026080406301722000_2026.07.30.741859v1.51","doi-asserted-by":"publisher","DOI":"10.1016\/j.jmb.2022.167859"},{"key":"2026080406301722000_2026.07.30.741859v1.52","doi-asserted-by":"publisher","DOI":"10.1073\/pnas.2023487118"},{"key":"2026080406301722000_2026.07.30.741859v1.53","doi-asserted-by":"publisher","DOI":"10.1021\/bi701757v"},{"issue":"31","key":"2026080406301722000_2026.07.30.741859v1.54","doi-asserted-by":"crossref","first-page":"9485","DOI":"10.1021\/bi0605585","article-title":"Spatial Separation of \u03b2-Sheet Domains of \u03b2-Amyloid: Disruption of Each \u03b2-Sheet by N-Methyl Amino Acids","volume":"45","year":"2006","journal-title":"Biochemistry"},{"key":"2026080406301722000_2026.07.30.741859v1.55","doi-asserted-by":"publisher","DOI":"10.1021\/ja0551382"},{"issue":"10","key":"2026080406301722000_2026.07.30.741859v1.56","doi-asserted-by":"crossref","first-page":"e202303007","DOI":"10.1002\/chem.202303007","article-title":"Structural Impact of N-terminal Pyroglutamate in an Amyloid-\u03b2(3-42) Fibril Probed by Solid-State NMR Spectroscopy","volume":"30","year":"2024","journal-title":"Chemistry \u2013 A European Journal"},{"key":"2026080406301722000_2026.07.30.741859v1.57","doi-asserted-by":"crossref","unstructured":"Milchberg, M. H. ; Warmuth, O. A. ; Borcik, C. G. ; Dhavale, D. D. ; Wright, E. R. ; Kotzbauer, P. T. ; Rienstra, C. M ., Alpha-Synuclein Fibril Structures Cluster into Distinct Classes. bioRxiv 2025, 2025.04.30.651534.","DOI":"10.1101\/2025.04.30.651534"},{"issue":"24","key":"2026080406301722000_2026.07.30.741859v1.58","doi-asserted-by":"crossref","first-page":"6210","DOI":"10.1002\/anie.201302065","article-title":"Expressed Protein Ligation at Methionine: N-Terminal Attachment of Homocysteine, Ligation, and Masking","volume":"52","year":"2013","journal-title":"Angewandte Chemie International Edition"},{"issue":"3","key":"2026080406301722000_2026.07.30.741859v1.59","doi-asserted-by":"crossref","first-page":"640","DOI":"10.1021\/acschembio.9b01038","article-title":"Chemoenzymatic Semisynthesis of Phosphorylated \u03b1-Synuclein Enables Identification of a Bidirectional Effect on Fibril Formation","volume":"15","year":"2020","journal-title":"ACS Chemical Biology"},{"key":"2026080406301722000_2026.07.30.741859v1.60","doi-asserted-by":"publisher","DOI":"10.1016\/j.cbpa.2021.04.011"}],"container-title":[],"original-title":[],"link":[{"URL":"https:\/\/syndication.highwire.org\/content\/doi\/10.64898\/2026.07.30.741859","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2026,8,4]],"date-time":"2026-08-04T13:30:35Z","timestamp":1785850235000},"score":1,"resource":{"primary":{"URL":"http:\/\/biorxiv.org\/lookup\/doi\/10.64898\/2026.07.30.741859"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2026,7,31]]},"references-count":60,"URL":"https:\/\/doi.org\/10.64898\/2026.07.30.741859","relation":{},"subject":[],"published":{"date-parts":[[2026,7,31]]},"subtype":"preprint"}}