However, these traditional techniques are limited by their sample preparation requirements, preventing their application towards large and dynamic protein complexes. The vast majority of structural information to date has been contributed by X-ray crystallography and nuclear magnetic resonance (NMR) spectroscopy, cumulatively totaling over 98% of all Protein Data Bank (PDB) entries (89% and 9%, respectively).
Thus, a detailed understanding of the structure and dynamics of these multimeric and functional entities is critical towards understanding their biological functions. Protein-protein interactions are fundamental to the formation of intricate interaction networks and the assembly of multisubunit protein complexes that represent the functional workhorses of the cell.
0 kommentar(er)
