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wave hplc nucleic acid fragment analysis system  (Transgenomic)

 
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    Transgenomic wave hplc nucleic acid fragment analysis system
    A lysine residue affect trinucleotide specificity of CD1454. ( a ) Alignment of the α2–α3 region of the zinc-binding domain of primases with characterized trinucleotide specificity. Predicted secondary structure (α helix in grey, β sheet in white) is indicated above the alignment. Ftula, Francisella tularensis; Ecoli, Escherichia coli ; Ypest, Yersinia pestis ; Paeru, Pseudomonas aeruginosa ; Cdiff, Clostridium difficile ; Aaeol, Aquifex aeolicus ; Saure, Staphylococcus aureus ; Cperf, Clostridium perfringens ; Gstea, Geobacillus stearothermophilus ; Banth, Bacillus anthracis ; Bsubt, Bacillus subtilis . Highlighted are the zinc coordinating residues of the CHC2 zinc-binding motif (yellow), and the adjacent histidine (green) or lysine (red) residues. Sequence conservation is indicated below the alignment. ( b ) Ribbon representation of the CD1454 primase zinc-binding domain indicating the zinc coordinating residues (yellow) and the location of the lysine residue (red). ( c ) Thermally denaturing high-performance liquid chromatography analysis of primase activity of wild-type (WT) and K70H mutant CD1454 primase protein with the CCC and CTA containing templates. The primase (WT or K70H mutant) and initiation trinucleotide in the single-stranded 23-mer template used is shown in the upper left corner of the respective chromatogram. The numbers in the panel to the right of the chromatograms denote the total peak area for the RNA primer products synthesized and shown in the associated chromatogram to the left. The mutation affects RNA primer synthesis from both preferred 5′-d(CCC) and non-preferred 5′-d(CTA) trinucleotides but shows the strongest increase in activity from the 5′-d(CTA) trinucleotide.
    Wave Hplc Nucleic Acid Fragment Analysis System, supplied by Transgenomic, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/wave hplc nucleic acid fragment analysis system/product/Transgenomic
    Average 90 stars, based on 1 article reviews
    wave hplc nucleic acid fragment analysis system - by Bioz Stars, 2026-05
    90/100 stars

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    1) Product Images from "Primase is required for helicase activity and helicase alters the specificity of primase in the enteropathogen Clostridium difficile"

    Article Title: Primase is required for helicase activity and helicase alters the specificity of primase in the enteropathogen Clostridium difficile

    Journal: Open Biology

    doi: 10.1098/rsob.160272

    A lysine residue affect trinucleotide specificity of CD1454. ( a ) Alignment of the α2–α3 region of the zinc-binding domain of primases with characterized trinucleotide specificity. Predicted secondary structure (α helix in grey, β sheet in white) is indicated above the alignment. Ftula, Francisella tularensis; Ecoli, Escherichia coli ; Ypest, Yersinia pestis ; Paeru, Pseudomonas aeruginosa ; Cdiff, Clostridium difficile ; Aaeol, Aquifex aeolicus ; Saure, Staphylococcus aureus ; Cperf, Clostridium perfringens ; Gstea, Geobacillus stearothermophilus ; Banth, Bacillus anthracis ; Bsubt, Bacillus subtilis . Highlighted are the zinc coordinating residues of the CHC2 zinc-binding motif (yellow), and the adjacent histidine (green) or lysine (red) residues. Sequence conservation is indicated below the alignment. ( b ) Ribbon representation of the CD1454 primase zinc-binding domain indicating the zinc coordinating residues (yellow) and the location of the lysine residue (red). ( c ) Thermally denaturing high-performance liquid chromatography analysis of primase activity of wild-type (WT) and K70H mutant CD1454 primase protein with the CCC and CTA containing templates. The primase (WT or K70H mutant) and initiation trinucleotide in the single-stranded 23-mer template used is shown in the upper left corner of the respective chromatogram. The numbers in the panel to the right of the chromatograms denote the total peak area for the RNA primer products synthesized and shown in the associated chromatogram to the left. The mutation affects RNA primer synthesis from both preferred 5′-d(CCC) and non-preferred 5′-d(CTA) trinucleotides but shows the strongest increase in activity from the 5′-d(CTA) trinucleotide.
    Figure Legend Snippet: A lysine residue affect trinucleotide specificity of CD1454. ( a ) Alignment of the α2–α3 region of the zinc-binding domain of primases with characterized trinucleotide specificity. Predicted secondary structure (α helix in grey, β sheet in white) is indicated above the alignment. Ftula, Francisella tularensis; Ecoli, Escherichia coli ; Ypest, Yersinia pestis ; Paeru, Pseudomonas aeruginosa ; Cdiff, Clostridium difficile ; Aaeol, Aquifex aeolicus ; Saure, Staphylococcus aureus ; Cperf, Clostridium perfringens ; Gstea, Geobacillus stearothermophilus ; Banth, Bacillus anthracis ; Bsubt, Bacillus subtilis . Highlighted are the zinc coordinating residues of the CHC2 zinc-binding motif (yellow), and the adjacent histidine (green) or lysine (red) residues. Sequence conservation is indicated below the alignment. ( b ) Ribbon representation of the CD1454 primase zinc-binding domain indicating the zinc coordinating residues (yellow) and the location of the lysine residue (red). ( c ) Thermally denaturing high-performance liquid chromatography analysis of primase activity of wild-type (WT) and K70H mutant CD1454 primase protein with the CCC and CTA containing templates. The primase (WT or K70H mutant) and initiation trinucleotide in the single-stranded 23-mer template used is shown in the upper left corner of the respective chromatogram. The numbers in the panel to the right of the chromatograms denote the total peak area for the RNA primer products synthesized and shown in the associated chromatogram to the left. The mutation affects RNA primer synthesis from both preferred 5′-d(CCC) and non-preferred 5′-d(CTA) trinucleotides but shows the strongest increase in activity from the 5′-d(CTA) trinucleotide.

    Techniques Used: Residue, Binding Assay, Sequencing, High Performance Liquid Chromatography, Activity Assay, Mutagenesis, Synthesized



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    A lysine residue affect trinucleotide specificity of CD1454. ( a ) Alignment of the α2–α3 region of the zinc-binding domain of primases with characterized trinucleotide specificity. Predicted secondary structure (α helix in grey, β sheet in white) is indicated above the alignment. Ftula, Francisella tularensis; Ecoli, Escherichia coli ; Ypest, Yersinia pestis ; Paeru, Pseudomonas aeruginosa ; Cdiff, Clostridium difficile ; Aaeol, Aquifex aeolicus ; Saure, Staphylococcus aureus ; Cperf, Clostridium perfringens ; Gstea, Geobacillus stearothermophilus ; Banth, Bacillus anthracis ; Bsubt, Bacillus subtilis . Highlighted are the zinc coordinating residues of the CHC2 zinc-binding motif (yellow), and the adjacent histidine (green) or lysine (red) residues. Sequence conservation is indicated below the alignment. ( b ) Ribbon representation of the CD1454 primase zinc-binding domain indicating the zinc coordinating residues (yellow) and the location of the lysine residue (red). ( c ) Thermally denaturing high-performance liquid chromatography analysis of primase activity of wild-type (WT) and K70H mutant CD1454 primase protein with the CCC and CTA containing templates. The primase (WT or K70H mutant) and initiation trinucleotide in the single-stranded 23-mer template used is shown in the upper left corner of the respective chromatogram. The numbers in the panel to the right of the chromatograms denote the total peak area for the RNA primer products synthesized and shown in the associated chromatogram to the left. The mutation affects RNA primer synthesis from both preferred 5′-d(CCC) and non-preferred 5′-d(CTA) trinucleotides but shows the strongest increase in activity from the 5′-d(CTA) trinucleotide.
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    A lysine residue affect trinucleotide specificity of CD1454. ( a ) Alignment of the α2–α3 region of the zinc-binding domain of primases with characterized trinucleotide specificity. Predicted secondary structure (α helix in grey, β sheet in white) is indicated above the alignment. Ftula, Francisella tularensis; Ecoli, Escherichia coli ; Ypest, Yersinia pestis ; Paeru, Pseudomonas aeruginosa ; Cdiff, Clostridium difficile ; Aaeol, Aquifex aeolicus ; Saure, Staphylococcus aureus ; Cperf, Clostridium perfringens ; Gstea, Geobacillus stearothermophilus ; Banth, Bacillus anthracis ; Bsubt, Bacillus subtilis . Highlighted are the zinc coordinating residues of the CHC2 zinc-binding motif (yellow), and the adjacent histidine (green) or lysine (red) residues. Sequence conservation is indicated below the alignment. ( b ) Ribbon representation of the CD1454 primase zinc-binding domain indicating the zinc coordinating residues (yellow) and the location of the lysine residue (red). ( c ) Thermally denaturing high-performance liquid chromatography analysis of primase activity of wild-type (WT) and K70H mutant CD1454 primase protein with the CCC and CTA containing templates. The primase (WT or K70H mutant) and initiation trinucleotide in the single-stranded 23-mer template used is shown in the upper left corner of the respective chromatogram. The numbers in the panel to the right of the chromatograms denote the total peak area for the RNA primer products synthesized and shown in the associated chromatogram to the left. The mutation affects RNA primer synthesis from both preferred 5′-d(CCC) and non-preferred 5′-d(CTA) trinucleotides but shows the strongest increase in activity from the 5′-d(CTA) trinucleotide.

    Journal: Open Biology

    Article Title: Primase is required for helicase activity and helicase alters the specificity of primase in the enteropathogen Clostridium difficile

    doi: 10.1098/rsob.160272

    Figure Lengend Snippet: A lysine residue affect trinucleotide specificity of CD1454. ( a ) Alignment of the α2–α3 region of the zinc-binding domain of primases with characterized trinucleotide specificity. Predicted secondary structure (α helix in grey, β sheet in white) is indicated above the alignment. Ftula, Francisella tularensis; Ecoli, Escherichia coli ; Ypest, Yersinia pestis ; Paeru, Pseudomonas aeruginosa ; Cdiff, Clostridium difficile ; Aaeol, Aquifex aeolicus ; Saure, Staphylococcus aureus ; Cperf, Clostridium perfringens ; Gstea, Geobacillus stearothermophilus ; Banth, Bacillus anthracis ; Bsubt, Bacillus subtilis . Highlighted are the zinc coordinating residues of the CHC2 zinc-binding motif (yellow), and the adjacent histidine (green) or lysine (red) residues. Sequence conservation is indicated below the alignment. ( b ) Ribbon representation of the CD1454 primase zinc-binding domain indicating the zinc coordinating residues (yellow) and the location of the lysine residue (red). ( c ) Thermally denaturing high-performance liquid chromatography analysis of primase activity of wild-type (WT) and K70H mutant CD1454 primase protein with the CCC and CTA containing templates. The primase (WT or K70H mutant) and initiation trinucleotide in the single-stranded 23-mer template used is shown in the upper left corner of the respective chromatogram. The numbers in the panel to the right of the chromatograms denote the total peak area for the RNA primer products synthesized and shown in the associated chromatogram to the left. The mutation affects RNA primer synthesis from both preferred 5′-d(CCC) and non-preferred 5′-d(CTA) trinucleotides but shows the strongest increase in activity from the 5′-d(CTA) trinucleotide.

    Article Snippet: For the denaturing HPLC analyses, a gradient 0–8.8% v/v acetonitrile over 16 min was used to obtain optimal separation of primer products and ssDNA templates on a WAVE HPLC nucleic acid fragment analysis system equipped with a DNA Sep HPLC column (Transgenomic; Omaha, NE, USA).

    Techniques: Residue, Binding Assay, Sequencing, High Performance Liquid Chromatography, Activity Assay, Mutagenesis, Synthesized