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. 2014 Dec 1;9(12):e113895. doi: 10.1371/journal.pone.0113895

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© 2014 Kalimeri et al

This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are properly credited.

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In the upper part of the figure we report the RMSD computed using the backbone heavy atoms of the residues that form the catalytic pocket of (upper graphs) and (bottom graphs) w.r.t. those of the apo and holo forms of lactate dehydrogenase at 300 K (left) and 360 K (right). In the lower part of the figure we present a pictorial representation of the conformational states accessible by the proteins when considered as function of the distance with respect to LDH apo and holo conformers. In green we sketched the two states visited by the MalDH, one characterized by an open conformation of the binding site loop and the other associated to a closed state. The MalDH (orange) is instead tightly confined in a closed state.

Inline graphic — In the upper part of the figure we report the RMSD computed using the backbone heavy atoms of the residues that form the catalytic pocket of (upper graphs) and (bottom graphs) w.r.t. those of the apo and holo forms of lactate dehydrogenase at 300 K (left) and 360 K (right). In the lower part of the figure we present a pictorial representation of the conformational states accessible by the proteins when considered as function of the distance with respect to LDH apo and holo conformers. In green we sketched the two states visited by the MalDH, one characterized by an open conformation of the binding site loop and the other associated to a closed state. The MalDH (orange) is instead tightly confined in a closed state.