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The choice of the phenylalanine mutants was based on the structural studies described below.
Because of the ease of using lesion length as a quantitative trait, our initial screen for gain-of-resistance mutants was based on reaction to bacterial blight.
Previously, the method used to screen Al-sensitive mutants was based on the measurement of root length of each plant before and after Al treatment.
The strategy for selecting these mutants was based upon the presence of opposite charges on their side-chain at neutral pH, their position at the AChE586-599 termini and their fibrilization properties (see above).
The construction of acyltransferase deletion mutants was based on the gene deletion strategy described by Wach [29].
The design of the mutants was based on a structure-activity relationship study of penetratin that led us to perform a R16A and a K13A/R16A exchange [ 46].
Similar(50)
Deletion mutants were based on the 3D structure in solution [19], [20].
Note that the numbering used for these mutants is based on the mitochondrial UNG1, which includes a 9 residue N-terminal mitochondrial localization signal, which is subsequently cleaved off [50].
Briefly, all mutants are based on a triple-auxotrophic (trp1Δ, leu2Δ, his3Δ) derivative of the C. glabrata ATCC 2001 reference strain.
These mutants were based on CVS11 pseudotype viruses, each containing a separate replacement of one of the 4 major antigenic sites by the corresponding region from a phylogroup II virus (LBV.Nig56-RV1).
It is important to note that the experimental rates for these mutants are based on steady-state data, and kcat may represent different properties in these mutants compared with the wild-type enzyme or other mutants (as the rate-limiting step may have changed from hydrolysis to alkylation).
Related(20)
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