ID #1558

Going off the question above of the question about polarity of the tubulin dimers..Does the difference in the status of ATP (whether it is hydrolyzed at the minus end or not hydrolyzed at the plus end) make the dimers have a different appearance?

First, be careful that you recognize what nucleotide binds in the nucleotide binding sites of tubulin dimers. But think about this logically... if being polar in this context means one side looks different than another, and these building blocks have a specific spot for binding a nucleotide, then wouldn't that part have looked different even before the nucleotide bound there?

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