Fibrinogen is a soluble blood plasma protein that supplies the building material for fibrin during coagulation. Thrombin cleaves small fibrinopeptides from fibrinogen, exposing sites that allow the resulting fibrin units to associate. The cleavage is a chemical trigger for assembly; forming the network also requires interactions between different protein molecules.[ref]
Thrombin EC 3.4.21.5 in IUBMB Enzyme Nomenclature. Reaction and comments: fibrinopeptide release and fibrin formation
A single-molecule experiment used optical tweezers to bring prepared protein partners together and measure their separation forces. Exposing the “A” binding knobs in fibrin produced strong specific interactions with complementary sites in fibrinogen or its end fragment. A competing peptide that mimicked the exposed knob suppressed those interactions, providing a control for binding-site specificity.[ref]
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