What is he best known for?
The fields of study he is best known for:
His main research concerns Stereochemistry, Protein structure, Active site, Biochemistry and Crystallography.
His study in Stereochemistry is interdisciplinary in nature, drawing from both Cofactor, Binding site, Thioredoxin, Ribonucleotide reductase and Alcohol dehydrogenase.
His Binding site research is multidisciplinary, relying on both Molecule and Substrate.
His research integrates issues of Dimer and Nicotinamide in his study of Alcohol dehydrogenase.
Within one scientific family, Hans Eklund focuses on topics pertaining to Hydrogen bond under Active site, and may sometimes address concerns connected to Random hexamer, Dioxygenase, Electron transfer and Denticity.
The concepts of his Crystallography study are interwoven with issues in Thioredoxin fold, Antiparallel, Beta sheet and Protein secondary structure.
His most cited work include:
- Three-dimensional structure of the free radical protein of ribonucleotide reductase (646 citations)
- 3 Alcohol Dehydrogenases (623 citations)
- Three-dimensional structure of horse liver alcohol dehydrogenase at 2.4 Å resolution (611 citations)
What are the main themes of his work throughout his whole career to date?
Hans Eklund mostly deals with Stereochemistry, Biochemistry, Active site, Enzyme and Alcohol dehydrogenase.
Hans Eklund has researched Stereochemistry in several fields, including Crystallography, Cofactor, Protein structure, Ribonucleotide reductase and Binding site.
His Crystallography study combines topics in areas such as Dimer, Crystallization and Hydrogen bond.
His Active site research includes themes of Antiparallel, Protein secondary structure, Mutant, Cysteine and Conformational change.
The Enzyme study combines topics in areas such as Residue, Protein primary structure and Protein quaternary structure.
His Alcohol dehydrogenase research integrates issues from Nicotinamide and NAD+ kinase, Alcohol oxidoreductase, Coenzyme binding.
He most often published in these fields:
- Stereochemistry (54.62%)
- Biochemistry (53.08%)
- Active site (38.46%)
What were the highlights of his more recent work (between 2001-2011)?
- Biochemistry (53.08%)
- Active site (38.46%)
- Stereochemistry (54.62%)
In recent papers he was focusing on the following fields of study:
Hans Eklund spends much of his time researching Biochemistry, Active site, Stereochemistry, Kinase and Enzyme.
His Active site research focuses on Crystallography and how it connects with Electron transfer, Photosystem I, Ligand and Electron transport chain.
His research in Stereochemistry intersects with topics in Oxidoreductase, Substrate, Dioxygenase, Protein structure and Binding site.
His Binding site research focuses on Protein subunit and how it relates to ATPase, Plasma protein binding, Allosteric regulation and Allosteric enzyme.
His Kinase study which covers Nucleoside analogue that intersects with Mutation.
His work investigates the relationship between Enzyme and topics such as Protein quaternary structure that intersect with problems in Bacillus anthracis, Alcohol, NAD-dependent alcohol dehydrogenase and Escherichia coli.
Between 2001 and 2011, his most popular works were:
- Crystal structure of naphthalene dioxygenase: side-on binding of dioxygen to iron. (363 citations)
- Structure and function of cellular deoxyribonucleoside kinases. (243 citations)
- Crystal Structure of E.Coli Alcohol Dehydrogenase Yqhd: Evidence of a Covalently Modified Nadp Coenzyme (145 citations)
In his most recent research, the most cited papers focused on:
His primary areas of investigation include Biochemistry, Protein structure, Stereochemistry, Ferredoxin and Oxidoreductase.
Many of his studies on Biochemistry involve topics that are commonly interrelated, such as Mesophile.
His studies in Protein structure integrate themes in fields like Plasma protein binding, ATPase, Thymidine and Protein subunit.
His Stereochemistry study integrates concerns from other disciplines, such as Molecule, Catalysis and Dioxygenase.
He focuses mostly in the field of Oxidoreductase, narrowing it down to topics relating to Cofactor and, in certain cases, Covalent bond, Dimer, Dehydrogenase and Alcohol dehydrogenase.
His Electron transfer research is multidisciplinary, incorporating perspectives in Crystallography and Active site.
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