Assessing complex protein-solvent interactions using environment-controlled crack-growth experiments

Assessing complex protein-solvent interactions using environment-controlled crack-growth experiments | 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 Research Article Assessing complex protein-solvent interactions using environment-controlled crack-growth experiments Tristan Baumberger, Olivier Ronsin This is a preprint; it has not been peer reviewed by a journal. https://doi.org/ 10.21203/rs.3.rs-5013815/v1 This work is licensed under a CC BY 4.0 License Status: Published Journal Publication published 10 Jan, 2025 Read the published version in International Journal of Fracture → Version 1 posted 9 You are reading this latest preprint version Abstract The modulation of protein functionality, i.e. their ability to fold/unfold, by adding low molecular weight substances to the “natural” solvent water is an important issue in biochemistry. Taking advantage of the unique ability of gelatin to self assemble into elastic networks via partial renaturation of the native collagen protein, we propose to recast the issue into a fracture mechanics one. We describe a method to decipher the effect of alcohols as cosolvents on gelatin networks from the shift of fracture energy in response to an environmental shock. After suitable subtraction of the viscous dissipation we are able characterize the solvent/network interaction by the relative shift of the free energy characteristic of the crosslinked→dismanteled transition of the network associated to its fracture. Using two alcohols, methanol and glycerol, we show that our method is able to accounts for their known contrasting effects on proteins. We briefly discuss the nature of the energy of interaction. In addition we unveil an open issue regarding the origin and consequence of the poroelastic solvent flow associated to crack propagation in hydrogels. Poroelasticity Fracture Mechanics Hydrogels Protein physics Full Text Additional Declarations No competing interests reported. Cite Share Download PDF Status: Published Journal Publication published 10 Jan, 2025 Read the published version in International Journal of Fracture → Version 1 posted Editorial decision: Revision requested 10 Oct, 2024 Reviews received at journal 10 Oct, 2024 Reviews received at journal 01 Oct, 2024 Reviewers agreed at journal 08 Sep, 2024 Reviewers agreed at journal 03 Sep, 2024 Reviewers invited by journal 02 Sep, 2024 Editor assigned by journal 02 Sep, 2024 Submission checks completed at journal 02 Sep, 2024 First submitted to journal 01 Sep, 2024 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. 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