Sentence examples for polymerase efficiency from inspiring English sources

Analysis of phage DNA sequences upstream of stx2 in four O157 H7 genome strains of clades 1, 2, 3, and 8, demonstrated that sequence variation is not likely to play a role in the differential transcription of Stx2; no SNPs were identified in phage DNA regions known to influence RNA polymerase efficiency and stx2 transcription [21].

The results were indistinguishable, thus suggesting that modification did not greatly influence polymerase efficiency.

However, this may not be the case if small differences in primer hybridization or polymerase efficiency exist between alleles.

The purpose of primer extension experiments was to determine the impact of lesion-induced conformational heterogeneity on the polymerase efficiency during TLS.

This N-terminal truncation variant displayed considerable enhancement only in Mg2+-dependent polymerase efficiency but without any alteration in Mn2+-dependent efficiency.

The first type is the defective variant (R96G), which is severely impaired in both Mg2+- and Mn2+-dependent polymerase efficiencies for both normal synthesis and lesion bypass.

The last type is the "wild-type-like" variants (Δ17, I261M, E276K, and Y374N), which retain both normal and TLS polymerase efficiencies similar to those of wild-type in the presence of either Mg2+ or Mn2+.

The six germline pol ι variants characterized in this study can be classified into three types according to the changes of relative polymerase efficiencies opposite G and the lesions in the presence of the added metal (Mg2+ or Mn2+) compared to wild-type (Tables 2– 7).

However, when long distance PCR (>5 kbp) was performed with KOD DNA polymerase, amplification efficiency (product yield) becomes lower because of its strong 3′ 5′ exonuclease activity for proof-reading.

The effect of the 2′-O-allyl substitution on cap analog has been evaluated with respect to its in vitro transcription by using T7 RNA polymerase, capping efficiency, and translational activity.

To determine if ETVr substitutions also negatively affected HBV polymerase catalytic efficiency, we determined the estimated kcat or turnover number as a measure of the number of reaction complexes that could be converted to product, per molecule of enzyme per unit of time.