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Evaluating the claim across its stated biological scope therefore depends on all-atom cyclic MD simulations of alpha-helices in explicit water and published cyclic AFM or macrorheology studies on intermediate filament networks and keratin fibers. Those resources exist in the literature and standard MD packages can test single-helix refolding at 300 K, but network-level experimental cyclic recovery data are scattered and confounded by inter-filament sliding. https://w3id.org/delphi/resource/assessment/buehler-2009-helical-networks-11--gemini http://purl.org/dc/terms/subject https://w3id.org/delphi/resource/concept/dataset-resolvability-0.2.0 https://w3id.org/delphi/resource/assessment/buehler-2009-helical-networks-11--gemini http://www.w3.org/1999/02/22-rdf-syntax-ns#type https://w3id.org/delphi/ontology/LLMClaimAssessment https://w3id.org/delphi/resource/assessment/buehler-2009-helical-networks-11--gemini http://www.w3.org/2000/01/rdf-schema#comment Proposed test with existing data: Subject alpha-helical filaments and intermediate-filament networks to cyclic loading-unloading protocols up to the unfolding plateau (prior to covalent bond rupture) at 300 K in all-atom MD or experimental rheology/AFM, measuring hysteresis loop recovery, alpha-helical hydrogen-bond reformation fraction, and residual strain after relaxation. 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