Sentence examples for mutant of ecDHFR from inspiring English sources

Consistent with these findings, a designed "humanized" mutant of ecDHFR switches binding specificity in the cell.

A clear example is ref (34) vs ref (18) with regard to the N23PP mutant of ecDHFR, where the second reproduced the findings of the first and also used a very similar analysis and interpretation of the temperature dependence of KIEs.

Enzyme KIEs and the framework of EA-VTST/MT have been used to study the N23PP/S148A mutant of EcDHFR, which does not present the millisecond-to-microsecond time scale motions observed in the M20 loop of wild-type EcDHFR and which displays a reduced hydride transfer rate constant.

A mutation in the Met20 loop of ecDHFR (N23PP or N23PP/S148A) inhibits the closed-to-occluded transition and also inhibits the sampling of productive higher-energy states on the millisecond time scale, as assayed by NMR relaxation dispersion.

Ile114 and Val115 are analogous to Val93 and Ile94, respectively, of ecDHFR.

The structural flexibility of BsDHFR has also been compared with that of EcDHFR.

Interestingly, the sequence of BsDHFR is more identical to that of the psychrophilic analogue MpDHFR than to that of EcDHFR.

Val119 displays a very high level of rotamer averaging in the occluded, but not the closed, complexes of ecDHFR.

Crystal structures of several complexes were solved by Kraut and co-workers, yielding insights into the structural mechanism of ecDHFR.

The nonequivalent Ile, Thr, and Val residues of hDHFR show an enhanced degree of rotameric averaging compared to that of the residues of ecDHFR, with an average pmajor of 0.68 ± 0.18 in hDHFR versus a value of 0.90 ± 0.07 in ecDHFR for the E FOL NADP+ complex (see Figure S6 of the Supporting Information for histograms of the pmajor distributions for hDHFR and ecDHFR E FOL NADP+ complexes).

N R2 relaxation dispersion experiments reveal conformational fluctuations on a millisecond time scale in all of the intermediates of the major enzymatic cycle of ecDHFR.