What is he best known for?
The fields of study he is best known for:
- Enzyme
- Amino acid
- Biochemistry
Zbigniew Dauter focuses on Stereochemistry, Active site, Hydrolase, Biochemistry and Crystallography.
His Stereochemistry research includes themes of Protein tertiary structure, Citrobacter freundii, Binding domain, Tyrosine phenol-lyase and Maltose.
His work deals with themes such as Nucleic acid sequence, Tyrosine, Pyridoxal, Serine and Cellulase, which intersect with Active site.
His Hydrolase study integrates concerns from other disciplines, such as Plasma protein binding, Binding site and Alpha-amylase.
His studies in Binding site integrate themes in fields like Peptide sequence, Sequence alignment, Escherichia coli and Histidine.
He combines subjects such as Hydrophobic effect, Streptomyces aureofaciens, Hydrogen bond and Anisotropy with his study of Crystallography.
His most cited work include:
- Molecular basis of agonism and antagonism in the oestrogen receptor. (2808 citations)
- The catalytic domain of Escherichia coli Lon protease has a unique fold and a Ser-Lys dyad in the active site. (158 citations)
- The Escherichia coli malonyl-CoA:acyl carrier protein transacylase at 1.5-A resolution. Crystal structure of a fatty acid synthase component. (155 citations)
What are the main themes of his work throughout his whole career to date?
Zbigniew Dauter mainly investigates Crystallography, Stereochemistry, Crystal structure, Molecule and Active site.
His Crystallography study incorporates themes from X-ray crystallography, Crystallization and Protein structure.
His research in Stereochemistry intersects with topics in Hydrolase, Amino acid, Biochemistry and Enzyme.
The study incorporates disciplines such as Electron transport chain, Catalase, Cofactor, Heme and Derivative in addition to Crystal structure.
His work is dedicated to discovering how Molecule, Crystal are connected with Ion and Synchrotron radiation and other disciplines.
His Active site course of study focuses on Protein subunit and Peptide sequence.
He most often published in these fields:
- Crystallography (58.24%)
- Stereochemistry (47.25%)
- Crystal structure (40.66%)
What were the highlights of his more recent work (between 1998-2014)?
- Stereochemistry (47.25%)
- Hydrolase (13.19%)
- Biochemistry (15.38%)
In recent papers he was focusing on the following fields of study:
Zbigniew Dauter mainly focuses on Stereochemistry, Hydrolase, Biochemistry, Binding site and Active site.
His research integrates issues of Non-covalent interactions, Molecule and Crystal structure in his study of Stereochemistry.
His Crystal structure study contributes to a more complete understanding of Crystallography.
His study on Hydrolase also encompasses disciplines like
- Catalytic triad and related Carboxylesterase, Protein structure and Cutinase,
- Glycoside hydrolase and related Amylase, Ligand, Tetrasaccharide, Bacillus halmapalus and Xylanase,
- Maltose which connect with Bacillus circulans, Alpha-amylase and Cyclodextrin glycosyltransferase.
His Binding site research includes elements of Histidine, Serine, Enzyme, Protein folding and Conformational change.
His research in Active site intersects with topics in Peptide bond, Nuclear magnetic resonance spectroscopy and Random hexamer.
Between 1998 and 2014, his most popular works were:
- The catalytic domain of Escherichia coli Lon protease has a unique fold and a Ser-Lys dyad in the active site. (158 citations)
- X-ray structure of Novamyl, the five-domain "maltogenic" alpha-amylase from Bacillus stearothermophilus: maltose and acarbose complexes at 1.7A resolution. (116 citations)
- Crystal structure of the Escherichia coli thioesterase II, a homolog of the human Nef binding enzyme. (107 citations)
In his most recent research, the most cited papers focused on:
The scientist’s investigation covers issues in Hydrolase, Biochemistry, Stereochemistry, Binding site and Active site.
His Hydrolase research is multidisciplinary, incorporating elements of Protein structure, Acarbose, Serine and Histidine.
Zbigniew Dauter combines subjects such as Catalytic triad and Carboxylesterase with his study of Protein structure.
The Serine study combines topics in areas such as Peptide bond, Random hexamer and Protein folding.
His study in Histidine is interdisciplinary in nature, drawing from both Peptide sequence, Sequence alignment, Plasma protein binding and Escherichia coli.
His work in Ntn hydrolase is not limited to one particular discipline; it also encompasses Crystal structure.
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