What is he best known for?
The fields of study he is best known for:
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 most cited work include:
- Escherichia coli maltose-binding protein is uncommonly effective at promoting the solubility of polypeptides to which it is fused. (827 citations)
- Tobacco etch virus protease: mechanism of autolysis and rational design of stable mutants with wild-type catalytic proficiency. (640 citations)
- The P1' specificity of tobacco etch virus protease. (299 citations)
What are the main themes of his work throughout his whole career to date?
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.
He most often published in these fields:
- Biochemistry (56.86%)
- Yersinia pestis (20.26%)
- Escherichia coli (17.65%)
What were the highlights of his more recent work (between 2015-2021)?
- Biochemistry (56.86%)
- Crystallography (15.03%)
- Crystal structure (14.38%)
In recent papers he was focusing on the following fields of 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.
Between 2015 and 2021, his most popular works were:
- Crystal structures of MBP fusion proteins. (32 citations)
- Removal of Affinity Tags with TEV Protease (24 citations)
- Insights Into the Allosteric Inhibition of the SUMO E2 Enzyme Ubc9. (14 citations)
In his most recent research, the most cited papers focused on:
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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