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clot levels. resolve the structural underpinnings on scales <1 nm (Hyeon et al., 2006a; Zhmurov et al., 2011). In contrast, biomolecularThe b- and g-nodules are homologous and each of them con-tains three crystallographically distinct globular domains (Yee et al., 1997; Spraggon et al., 1997; Brown et al., 2000; Madrazo and its derivatives. This paper is a significant advancement over previously published preliminary work on the unfolding of fibrinogen oligomers (Brown et al., 2007) with additional AFMet al., 2001). Fg is partially cleaved by thrombin, which triggers formation of a three-dimensional fibrous network called a fibrin clot (Weisel, 2005). experiments, including new molecular variants, and novel ap-proaches to data analysis and modeling. Importantly, the exper-imental measurements have been analyzed in comparison withINTRODUCTION Fibrin is a polymer that provides the scaffold for protective hemostatic plugs and obstructive thrombi. Human fibrin is formed from fibrinogen (Fg), a blood plasma protein, consistin