Abstract:Abstract. In order to elucidate the thermal properties of Thermus thermophilus 3-isopropylmalate dehydrogenase, mutant structures with mutations at the Cterminus were compared with each other. The structural movement can be anticipated from the structural changes among mutants in regions of a minor groove and pillar. Our previous studies revealed that the open-close movement of the active site groove antagonizes to that of the minor groove (like a paperclip) and the thermostability of the enzyme increases when… Show more
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