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Substrate-induced dimerization of engineered monomeric variants of triosephosphate isomerase from Trichomonas vaginalis
(2015-11)
"The dimeric nature of triosephosphate isomerases (TIMs) is maintained by an extensive surface area interface of more than 1600 angstrom 2. TIMs from Trichomonas vaginalis (TvTIM) are held in their dimeric state by two ...
A competent catalytic active site is necessary for substrate induced dimer assembly in triosephosphate isomerase
(Elsevier, 2017)
"The protozoan parasite Trichomonas vaginalis contains two nearly identical triosephosphate isomerases (TvTIMs) that dissociate into stable monomers and dimerize upon substrate binding. Herein, we compare the role of the ...