On Dimer and other multiples...

Case number:699969-997097
Opened by:bertro
Opened on:Monday, February 24, 2014 - 01:48
Last modified:Friday, February 28, 2014 - 00:51

Am I right in thinking that, in real life, all copies of a dimer would "move/position" their sidechains independently from the other copy and "not" in a "mirror like fashion" as we are seeing in foldit puzzles?


(Mon, 02/24/2014 - 01:48  |  4 comments)

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Exploiting symmetries like "mirror like fashion" lets two 65 residue monomers act more like a 65 residue puzzle than a 130 residue puzzle.

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Jeff gave the computer science answer (which is correct -- it's computationally far less expensive if we can exploit symmetry). The scientific answer is that nature actually exploits symmetry, which is why so many oligomeric proteins have evolved, and we're just emulating nature by exploiting symmetry ourselves.

Although it is technically true that every protein molecule can move independently of every other, subunits in an oligomer adopt near-identical conformations (side-chains and all), so it's scientifically valid to take a shortcut by enforcing perfect symmetry. I know it's counter-intuitive, but there is actually a physical basis for why the different subunits in a symmetric oligomer will have identical (or near-identical) conformations.

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