Improved detection of magnetic interactions in proteins based on long-lived coherences

Improved detection of magnetic interactions in proteins based on long-lived coherences | Research Square window.SnipcartSettings = { analytics: { enabled: false } }; (function() { var accessVector = localStorage.getItem('access_vector') || ''; window.dataLayer = window.dataLayer || []; if (accessVector) { window.dataLayer.push({ user: { profile: { profileInfo: { snid: accessVector } } } }); } })(); (function(w,d,s,l,i){w[l]=w[l]||[];w[l].push({'gtm.start':new Date().getTime(),event:'gtm.js'});var f=d.getElementsByTagName(s)[0],j=d.createElement(s),dl=l!='dataLayer'?'&l='+l:'';j.async=true;j.src='https://www.googletagmanager.com/gtm.js?id='+i+dl;f.parentNode.insertBefore(j,f);})(window,document,'script','dataLayer','GTM-K279D39R'); Browse Preprints In Review Journals COVID-19 Preprints AJE Video Bytes Research Tools Research Promotion AJE Professional Editing AJE Rubriq About Preprint Platform In Review Editorial Policies Our Team Advisory Board Help Center Sign In Submit a Preprint Cite Share Download PDF Article Improved detection of magnetic interactions in proteins based on long-lived coherences Aude Sadet, Octavian Ianc, Florin Teleanu, Andrei Ciumeică, Adonis Lupulescu, and 1 more This is a preprint; it has not been peer reviewed by a journal. https://doi.org/ 10.21203/rs.3.rs-3694602/v1 This work is licensed under a CC BY 4.0 License Status: Published Journal Publication published 16 May, 2024 Read the published version in Communications Chemistry → Version 1 posted You are reading this latest preprint version Abstract Living systems rely on molecular building blocks with low structural symmetry. Therefore, the constituent amino-acids and nucleotides yield short-lived nuclear magnetic responses to electromagnetic radiation. Magnetic signals are at the basis of molecular imaging, structure determination and interaction studies in the liquid state. Interactions between magnetic nuclei can only be detected provided the lifetimes of spin order are sufficient. In J -coupled pairs of nuclei, long-lived coherences (LLC’s) can be excited between states with different spin-permutation symmetry. In solution state, as the molecular weight of analytes increases, coherences with long lifetimes are needed to yield advantageous through-space magnetisation transfers. In protein Lysozyme, weighing 14.3 kDa, we sustained coherences with lifetimes twice as long as those of classical magnetisation for the aliphatic protons of glycine residues. We found that, in this protein of significant molecular weight, LLC’s yield substantial through-space magnetisation transfers: in agreement with theory, spin-order transfer stemming from LLC’s overcame transfers from classical coherences by factors 2-3. Furthermore, the permutation symmetry of LLC-based transfers allowed mapping the positions of interacting atoms in the protein structure with respect to the molecular plane of glycine residues in a stereospecific manner. These findings can extend the scope of liquid-state high-resolution spectroscopy in the analysis of biomolecular complexes of high molecular weight. Biological sciences/Structural biology/NMR spectroscopy/Solution-state NMR Physical sciences/Chemistry/Physical chemistry/Chemical physics Full Text Additional Declarations There is NO Competing Interest. Supplementary Files SILLCLysozyme1XIIASF.pdf Cite Share Download PDF Status: Published Journal Publication published 16 May, 2024 Read the published version in Communications Chemistry → Version 1 posted You are reading this latest preprint version Research Square lets you share your work early, gain feedback from the community, and start making changes to your manuscript prior to peer review in a journal. As a division of Research Square Company, we’re committed to making research communication faster, fairer, and more useful. We do this by developing innovative software and high quality services for the global research community. Our growing team is made up of researchers and industry professionals working together to solve the most critical problems facing scientific publishing. Also discoverable on Platform About Our Team In Review Editorial Policies Advisory Board Help Center Resources Author Services Accessibility API Access RSS feed Manage Cookie Preferences © Research Square 2026 | ISSN 2693-5015 (online) Privacy Policy Terms of Service Do Not Sell My Personal Information {"props":{"pageProps":{"initialData":{"identity":"rs-3694602","acceptedTermsAndConditions":true,"allowDirectSubmit":false,"archivedVersions":[],"articleType":"Article","associatedPublications":[],"authors":[{"id":260044893,"identity":"71eb7702-a2e4-41f5-adfa-4c129f7f9827","order_by":0,"name":"Aude 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Portfolio","twitterHandle":"","acdcEnabled":false,"dfaEnabled":false,"editorialSystem":"ejp","reportingPortfolio":"","inReviewEnabled":true,"inReviewRevisionsEnabled":false},"keywords":"","lastPublishedDoi":"10.21203/rs.3.rs-3694602/v1","lastPublishedDoiUrl":"https://doi.org/10.21203/rs.3.rs-3694602/v1","license":{"name":"CC BY 4.0","url":"https://creativecommons.org/licenses/by/4.0/"},"manuscriptAbstract":"Living systems rely on molecular building blocks with low structural symmetry. Therefore, the constituent amino-acids and nucleotides yield short-lived nuclear magnetic responses to electromagnetic radiation. Magnetic signals are at the basis of molecular imaging, structure determination and interaction studies in the liquid state. Interactions between magnetic nuclei can only be detected provided the lifetimes of spin order are sufficient. In \u003ci\u003eJ\u003c/i\u003e-coupled pairs of nuclei, long-lived coherences (LLC’s) can be excited between states with different spin-permutation symmetry. In solution state, as the molecular weight of analytes increases, coherences with long lifetimes are needed to yield advantageous through-space magnetisation transfers. In protein Lysozyme, weighing 14.3 kDa, we sustained coherences with lifetimes twice as long as those of classical magnetisation for the aliphatic protons of glycine residues. We found that, in this protein of significant molecular weight, LLC’s yield substantial through-space magnetisation transfers: in agreement with theory, spin-order transfer stemming from LLC’s overcame transfers from classical coherences by factors 2-3. Furthermore, the permutation symmetry of LLC-based transfers allowed mapping the positions of interacting atoms in the protein structure with respect to the molecular plane of glycine residues in a stereospecific manner. 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