Dynamical protein interaction pathways: A molecular root to diseases

Dynamical protein interaction pathways: A molecular root to diseases | 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PDF Article Dynamical protein interaction pathways: A molecular root to diseases Paul Asir M This is a preprint; it has not been peer reviewed by a journal. https://doi.org/ 10.21203/rs.3.rs-4372634/v1 This work is licensed under a CC BY 4.0 License Status: Posted Version 1 posted You are reading this latest preprint version Abstract We propose a complex dynamical model to mimic the protein-protein interaction. The signalling pathways that activate the proteins enact the intracellular functions are modelled by random and complimentary linking. The molecular roots of diseases are illuminated on the grounds of protein misfolding. Specifically, amy-loid fibrillated states are emphasized that are analogous to the coalescence of ordered and disordered dynamics. Also, a β− pleated sheet can be inferred from the model reflected as an anti-phase synchronized state. Note that the coupling strength is equivalent to the electromagnetic forces of the individual molecules. Critical clustering coupling strength has been analytically derived. Statistical techniques are imposed to impart an energy perspective of the model. We found that the relaxation time of the model plays a vital role in protein folding. We quote that ‘The quicker the folding, the lesser the entropy’. We validate the model using pathological data of breast carcinoma obtained from https://proteinatlas.org . Biological sciences/Biophysics Biological sciences/Computational biology and bioinformatics Protein modeling Dynamical pathways Nonlinear dynamics Amyloid diseases Full Text Additional Declarations No competing interests reported. Cite Share Download PDF Status: Posted 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-4372634","acceptedTermsAndConditions":true,"allowDirectSubmit":true,"archivedVersions":[],"articleType":"Article","associatedPublications":[],"authors":[{"id":309700526,"identity":"d5a17f52-789d-411b-b4f2-ef14875df254","order_by":0,"name":"Paul Asir M","email":"data:image/png;base64,iVBORw0KGgoAAAANSUhEUgAAAZAAAAAyAQMAAABI0h/eAAAABlBMVEX///8AAABVwtN+AAAACXBIWXMAAA7EAAAOxAGVKw4bAAAA9ElEQVRIiWNgGAWjYHACxgOMDWC6geEDkGJjJ0IPXAvjDJAWZuK1MDAw84BJAsrN2c8YHC7ccZiBv/9w22ebX9vk+ZgZGD98zMGtxbInx+DwzDOHGSRuJDbPzu27bdjGzMAsOXMbbi0GB4BaeNsOMzDcYGxmzu25zQjUwsbMi0/L+TcQLfLnDzYzW/bcties5QbUFoMDic3MDD9uJxLUYjnjWcHhmW3pPIZAvzD2NtxObmNmbMbrF3P+5I2PC9us5eTOH3/M8OPPbdv57c0HP3zE5zAGcEQ0g2OEgbENTDbgVo/QUgfl/sGreBSMglEwCkYoAAB/yVQV7buqBQAAAABJRU5ErkJggg==","orcid":"","institution":"Mount Zion College of Engineering and Technology","correspondingAuthor":true,"prefix":"","firstName":"Paul","middleName":"Asir","lastName":"M","suffix":""}],"badges":[],"createdAt":"2024-05-05 17:25:56","currentVersionCode":1,"declarations":"","doi":"10.21203/rs.3.rs-4372634/v1","doiUrl":"https://doi.org/10.21203/rs.3.rs-4372634/v1","draftVersion":[],"editorialEvents":[],"editorialNote":"","failedWorkflow":false,"files":[{"id":65564374,"identity":"41e06d2a-93a2-41c8-a9f8-1cf74e6e7293","added_by":"auto","created_at":"2024-09-30 04:53:56","extension":"pdf","order_by":1,"title":"","display":"","copyAsset":false,"role":"manuscript-pdf","size":1473213,"visible":true,"origin":"","legend":"","description":"","filename":"ppimd.pdf","url":"https://assets-eu.researchsquare.com/files/rs-4372634/v1_covered_8ba75988-3252-486d-a261-c899a3c7cf71.pdf"}],"financialInterests":"No competing interests reported.","formattedTitle":"Dynamical protein interaction pathways: A molecular root to diseases","fulltext":[],"fulltextSource":"","fullText":"","funders":[],"hasAdminPriorityOnWorkflow":false,"hasManuscriptDocX":false,"hasOptedInToPreprint":true,"hasPassedJournalQc":"","hasAnyPriority":false,"hideJournal":true,"highlight":"","institution":"","isAcceptedByJournal":false,"isAuthorSuppliedPdf":true,"isDeskRejected":"","isHiddenFromSearch":false,"isInQc":false,"isInWorkflow":false,"isPdf":true,"isPdfUpToDate":true,"isWithdrawnOrRetracted":false,"journal":{"display":true,"email":"[email protected]","identity":"researchsquare","isNatureJournal":false,"hasQc":true,"allowDirectSubmit":true,"externalIdentity":"","sideBox":"","snPcode":"","submissionUrl":"/submission","title":"Research Square","twitterHandle":"researchsquare","acdcEnabled":true,"dfaEnabled":false,"editorialSystem":"","reportingPortfolio":"","inReviewEnabled":false,"inReviewRevisionsEnabled":true},"keywords":"Protein modeling , Dynamical pathways , Nonlinear dynamics , Amyloid diseases","lastPublishedDoi":"10.21203/rs.3.rs-4372634/v1","lastPublishedDoiUrl":"https://doi.org/10.21203/rs.3.rs-4372634/v1","license":{"name":"CC BY 4.0","url":"https://creativecommons.org/licenses/by/4.0/"},"manuscriptAbstract":"We propose a complex dynamical model to mimic the protein-protein interaction. 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