The tail of RNA polymerase II is flexible, not folded into a fixed structure , but does each repeat have more "rigid" structure (i.e. fold into a structure that has less rotation freedom inside a repeat)? If not, then how can the proteins bind some repeat with high specificity? (you can't make lock and key with soft material)

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    $\begingroup$ Please clarify. First provide a source for your statement, even if it is a textbook. Is “flexible” really the right word, or do you mean it has no fixed structure in a crystal of that protein alone. Second, what do you mean by secondary structure? The repeat is only seven amino acids — why would you think it would be alpha-helix or beta-sheet, and why do you think this is a requirement for protein–protein interaction. Your question seems to me to make a series of assumptions, the dubiety of which you don’t appear to realize. $\endgroup$
    – David
    Dec 1, 2020 at 20:12


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