Fibrinogen primary structure

There are several self-assembling macromolecules that are of interest to us in this text. They include (1) collagen, the primary structural material found in the extracellular matrix (2) actin, a component of the cell cytoskeleton that is involved in cell locomotion and in formation of the thin filaments of muscle (3) microtubules, which are involved in cell mitosis, movement, and organelle movement and finally (4) fibrinogen, which forms fibrin networks that minimize bleeding from cut vessels. Self-assembly is important in these systems because the function of these macromolecules can be modified via processes that increase the molecular axial ratio and hence decrease the solubility. 

The primary structures of two Asn-linked glycans from bovine fibrinogen have been determined by methylation analysis and NMR spectroscopy, and were also shown to be dianteimary [57]. 

The first principle of enzyme inhibitor design is Use aU the available information . This information can be biological, functional, structural, chemical, or theoretical. There is such an immense amount of biological information on thrombin that it cannot be surveyed here we focus on thrombin as a serine protease of the trypsin family and take fibrinogen to be its primary substrate. A convenient way to look at the information available is from the more general to the very specific. For thrombin, we may take four levels the general catalytic mechanism the particular substrate types processed the structure of the protein and, often forgotten, the flexibihty of the protein required to achieve this function. 

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