In larger protein complexes proteins are bound together encoded into precise binding interfaces. Specificity and affinity are the foundational aspects that make these binding interfaces possible. However there are stills problems that can arise within the system. Large disordered proteins are to still capable of binding to various sites along well-structures polypetides. The reasoning behind this anomoly is because of the large opposite net charge of the two proteins. Sequencing nalysis of multiple structures shows that this interaction occurs abbundantly throughout nature.
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