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The Journal of Biological Chemistry|April 22, 1994
A novel class of FokI restriction endonuclease mutants that cleave hemi-methylated substratesD S Waugh, R T SauerProtein Expression and Purification|December 27, 2011
Isolation of Metarhizium anisopliae carboxypeptidase A with native disulfide bonds from the cytosol of Escherichia coli BL21(DE3)Brian P Austin, David S WaughInfectious Diseases in Obstetrics and Gynecology|January 1, 1995
Doxycycline or ofloxacin for outpatient chlamydial pelvic inflammatory disease? A cost-benefit and cost-effectiveness analysisM J Rosenberg, M S WaughProtein Science : a Publication of the Protein Society|August 19, 1999
Escherichia coli maltose-binding protein is uncommonly effective at promoting the solubility of polypeptides to which it is fusedR B Kapust, D S WaughJournal of Bacteriology|November 1, 1990
Complementation of an RNase P RNA (rnpB) gene deletion in Escherichia coli by homologous genes from distantly related eubacteriaD S Waugh, N R PaceProtein Expression and Purification|June 30, 2000
Controlled intracellular processing of fusion proteins by TEV proteaseR B Kapust, D S WaughBiotechnology and Bioengineering|June 20, 2014
Unrelated solubility-enhancing fusion partners MBP and NusA utilize a similar mode of actionSreejith Raran-Kurussi, David S WaughProceedings of the National Academy of Sciences of the United States of America|October 15, 1993
Single amino acid substitutions uncouple the DNA binding and strand scission activities of Fok I endonucleaseD S Waugh, R T SauerPlos One|November 21, 2012
The ability to enhance the solubility of its fusion partners is an intrinsic property of maltose-binding protein but their folding is either spontaneous or chaperone-mediatedSreejith Raran-Kurussi, David S WaughAnalytical Biochemistry|April 24, 2016
A dual protease approach for expression and affinity purification of recombinant proteinsSreejith Raran-Kurussi, David S WaughPageof 20