An Unbiased Approach on The Conformational Dynamics of In-Solution Fibrinogen and Its Physiological Implications.



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By itself, Fibrinogen (Fng) stands out as one of the most complex hematopoietic proteins in the cardiovascular system for multiple species in nature. Upon its activation and further cascade mechanisms, Fng can polymerize into fibrin and contribute to blood clot formation and substantial growth. Fng’s interactions with fibrinolytic proteins aggregate into a conglomerate of different fragments in blood bodily mechanisms. Any form of dysregulation in any of these pathways can lead to several complications not only within the cardiovascular system but throughout the entirety of the body. Understanding the crux of Fng’s functions and interactions with itself along with other proteins ultimately can be traced back to its inherent dynamic structure. In this study, I aim to probe the intrinsic flexibility that is beset on Fng by way of its multi-domain composition, allowing it to withstand incredible mechanical forces as well as being highly dynamic in its physiological form. Thus, extending the key biological concept that structure and flexibility that comes with it determine functions. Through an unbiased approach by implementing protein structural studies as well as computational dynamic simulations, in-solution Fng dynamics were studied in their totality.



Fibrinogen, Fibrin, in-solution, coiled coil domain, globular regions, HDX-MS, Negative Stain Electromagnetic Imaging, Small Angle X-ray Scattering, X-ray crystallography, conformational dynamics, coagulation, platelet aggregation.