The scientist’s investigation covers issues in Biochemistry, Fusion protein, TEV protease, Protease and Tobacco etch virus. His study in Hydrolase, Enzyme activator, Zymogen, Vacuole and Peptide sequence is carried out as part of his Biochemistry studies. David S. Waugh works in the field of Fusion protein, namely Maltose-binding protein.
His Maltose-binding protein research includes elements of Thermotoga maritima, Thermophile, Bacteria and Protein folding. His TEV protease research incorporates elements of Polyhistidine-tag and Enzyme. His studies deal with areas such as Peptide, Viral protein, Autolysis and Tandem affinity purification as well as Protease.
His main research concerns Biochemistry, Yersinia pestis, Escherichia coli, Fusion protein and Maltose-binding protein. His multidisciplinary approach integrates Biochemistry and Tobacco etch virus in his work. He has researched Yersinia pestis in several fields, including Secretion, Virulence factor, Microbiology and Effector.
His Escherichia coli research integrates issues from Crystallography and Recombinant DNA. His work deals with themes such as Amino acid, Target protein and Expression vector, which intersect with Fusion protein. David S. Waugh has included themes like Inclusion bodies, Affinity chromatography, FLAG-tag and Protein folding in his Maltose-binding protein study.
His primary areas of study are Biochemistry, Crystallography, Crystal structure, Fragment and Maltose-binding protein. Biochemistry is a component of his Phosphatase, SUMO protein, Microarray, Protein tyrosine phosphatase and Phosphate studies. Peptide sequence, Protein Data Bank and Structural motif is closely connected to Protein structure in his research, which is encompassed under the umbrella topic of Crystallography.
Fusion protein and Recombinant DNA are closely tied to his Maltose-binding protein research. The study of Fusion protein is intertwined with the study of Escherichia coli in a number of ways. The study incorporates disciplines such as Enhancer and Protein folding in addition to Escherichia coli.
David S. Waugh mostly deals with Biochemistry, Maltose-binding protein, Small molecule, SUMO protein and Fusion protein. David S. Waugh performs multidisciplinary study in the fields of Biochemistry and Phosphothreonine binding via his papers. The Maltose-binding protein study combines topics in areas such as Dual-specificity phosphatase, Affinity chromatography and Protease.
His Protease research incorporates themes from Escherichia coli, Chromatography, Myc-tag, FLAG-tag and Tandem affinity purification. David S. Waugh interconnects Microarray, Binding site and Enzyme in the investigation of issues within SUMO protein. In general Fusion protein study, his work on TEV protease often relates to the realm of Protein crystallization, thereby connecting several areas of interest.
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Escherichia coli maltose-binding protein is uncommonly effective at promoting the solubility of polypeptides to which it is fused.
Rachel B. Kapust;David S. Waugh.
Protein Science (1999)
Tobacco etch virus protease: mechanism of autolysis and rational design of stable mutants with wild-type catalytic proficiency.
Rachel B. Kapust;József Tözsér;Jeffrey D. Fox;D.Eric Anderson.
Protein Engineering (2001)
The P1' specificity of tobacco etch virus protease.
Rachel B Kapust;József Tözsér;Terry D Copeland;David S Waugh.
Biochemical and Biophysical Research Communications (2002)
Expression and Purification of Soluble His 6 -Tagged TEV Protease
Joseph E. Tropea;Scott Cherry;David S. Waugh.
Methods of Molecular Biology (2009)
An overview of enzymatic reagents for the removal of affinity tags
David S. Waugh.
Protein Expression and Purification (2011)
Structural basis for the substrate specificity of tobacco etch virus protease.
Jason Phan;Alexander Zdanov;Artem G. Evdokimov;Joseph E. Tropea.
Journal of Biological Chemistry (2002)
The 8-nucleotide-long RNA:DNA hybrid is a primary stability determinant of the RNA polymerase II elongation complex.
Maria L. Kireeva;Natalia Komissarova;David S. Waugh;Mikhail Kashlev.
Journal of Biological Chemistry (2000)
Controlled intracellular processing of fusion proteins by TEV protease.
Rachel B. Kapust;David S. Waugh.
Protein Expression and Purification (2000)
Solubility-enhancing proteins MBP and NusA play a passive role in the folding of their fusion partners.
Sreedevi Nallamsetty;David S. Waugh.
Protein Expression and Purification (2006)
Gateway vectors for the production of combinatorially‐tagged His6‐MBP fusion proteins in the cytoplasm and periplasm of Escherichia coli
Sreedevi Nallamsetty;Brian P. Austin;Kerri J. Penrose;David S. Waugh.
Protein Science (2005)
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