Live-Cell Protein Engineering With An Ultra-Short Split Intein at Desiree Turner blog

Live-Cell Protein Engineering With An Ultra-Short Split Intein. Though efficient for in vitro applications, these. Using the shortest naturally occurring split intein, vidal, we report examples of traceless protein modification in live cells. Using the shortest naturally occurring split intein, vidal, we report examples of traceless protein modification in live cells. Histogram displaying the relative ic50 values of kanamycin for each of the extein mutants tested at the −1 (red), −2 (blue), and +2 (green) extein residues (mean ± sd, n = 3). In red) and atypically split (bottom; In vitro characterization of vidal. Split inteins are privileged molecular scaffolds for the chemical modification of proteins.

(a) Live cell bioorthogonal labeling scheme of overexpressed insulin
from www.researchgate.net

Using the shortest naturally occurring split intein, vidal, we report examples of traceless protein modification in live cells. Histogram displaying the relative ic50 values of kanamycin for each of the extein mutants tested at the −1 (red), −2 (blue), and +2 (green) extein residues (mean ± sd, n = 3). In vitro characterization of vidal. Split inteins are privileged molecular scaffolds for the chemical modification of proteins. Using the shortest naturally occurring split intein, vidal, we report examples of traceless protein modification in live cells. In red) and atypically split (bottom; Though efficient for in vitro applications, these.

(a) Live cell bioorthogonal labeling scheme of overexpressed insulin

Live-Cell Protein Engineering With An Ultra-Short Split Intein Split inteins are privileged molecular scaffolds for the chemical modification of proteins. Though efficient for in vitro applications, these. Using the shortest naturally occurring split intein, vidal, we report examples of traceless protein modification in live cells. Split inteins are privileged molecular scaffolds for the chemical modification of proteins. In red) and atypically split (bottom; In vitro characterization of vidal. Histogram displaying the relative ic50 values of kanamycin for each of the extein mutants tested at the −1 (red), −2 (blue), and +2 (green) extein residues (mean ± sd, n = 3). Using the shortest naturally occurring split intein, vidal, we report examples of traceless protein modification in live cells.

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