<p>(A) Native-PAGE. (B) Activity staining. (C) Stability at 95°C. The protein concentration was 1 mg/ml for the native-PAGE and activity staining analysis and 0.33 mg/ml for the stability experiments. The presented data were calculated from three repetitions.</p
<p>A. SEC chromatograms (Superdex 75 column) of FL-Bid, cBid and tBid. Black curves, soluble protein...
<p><b>A</b> Analysis of recombinant HAs with and without trimerization domain by reducing, denaturin...
<p>(A) Fractions from Peak 1 after purification of WT and His-D4/A20<sub>1–50</sub> mutants (see <a ...
<p>(A) 12.5% SDS-PAGE. (B) 10% native-PAGE. (C) Activity staining of the bands in native-PAGE. M is ...
College of Math and Physical Science Research Forum Award for Best Poster Presentation in Department...
Proteins are oligomeric macromolecules composed of amino acid monomers. Mutating specific amino resi...
Understanding how mutations affect protein activity and organismal fitness is a major challenge. We ...
<p>(a) Western blotting with anti-GFP antibody confirming the protein expression levels of wild-type...
Most single point mutations destabilize folded proteins. Mutations that stabilize a protein typicall...
<p><sup>a</sup>predicted protein thermal stability change (∆∆G in Kcal/mol) of mutation from CUPSAT ...
Proteins are macromolecules essential to all living organisms. They consist of amino acids linked to...
<p>Where, “WT” is the wild-type amino acid in the protein, “NEW” is the new amino acid after Mutatio...
<p>(A) Far-UV CD data for the thermally-induced denaturation of the native and refolded protein SBD5...
<p>The formation of active high-order oligomers is a reversible process, while the aggregation pathw...
Is it possible to compare the physicochemical properties of a wild-type protein and its mutant form ...
<p>A. SEC chromatograms (Superdex 75 column) of FL-Bid, cBid and tBid. Black curves, soluble protein...
<p><b>A</b> Analysis of recombinant HAs with and without trimerization domain by reducing, denaturin...
<p>(A) Fractions from Peak 1 after purification of WT and His-D4/A20<sub>1–50</sub> mutants (see <a ...
<p>(A) 12.5% SDS-PAGE. (B) 10% native-PAGE. (C) Activity staining of the bands in native-PAGE. M is ...
College of Math and Physical Science Research Forum Award for Best Poster Presentation in Department...
Proteins are oligomeric macromolecules composed of amino acid monomers. Mutating specific amino resi...
Understanding how mutations affect protein activity and organismal fitness is a major challenge. We ...
<p>(a) Western blotting with anti-GFP antibody confirming the protein expression levels of wild-type...
Most single point mutations destabilize folded proteins. Mutations that stabilize a protein typicall...
<p><sup>a</sup>predicted protein thermal stability change (∆∆G in Kcal/mol) of mutation from CUPSAT ...
Proteins are macromolecules essential to all living organisms. They consist of amino acids linked to...
<p>Where, “WT” is the wild-type amino acid in the protein, “NEW” is the new amino acid after Mutatio...
<p>(A) Far-UV CD data for the thermally-induced denaturation of the native and refolded protein SBD5...
<p>The formation of active high-order oligomers is a reversible process, while the aggregation pathw...
Is it possible to compare the physicochemical properties of a wild-type protein and its mutant form ...
<p>A. SEC chromatograms (Superdex 75 column) of FL-Bid, cBid and tBid. Black curves, soluble protein...
<p><b>A</b> Analysis of recombinant HAs with and without trimerization domain by reducing, denaturin...
<p>(A) Fractions from Peak 1 after purification of WT and His-D4/A20<sub>1–50</sub> mutants (see <a ...
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