Douglas H. Ohlendorf

What is he best known for?

The fields of study he is best known for:

• Enzyme
• Gene
• DNA

Douglas H. Ohlendorf mostly deals with Stereochemistry, Protein structure, Biochemistry, Repressor and DNA. His Stereochemistry study integrates concerns from other disciplines, such as Crystal structure, Active site, Dioxygenase, Catechol dioxygenase and Tetramer. His Active site research is multidisciplinary, relying on both Crystallography, Ligand and Binding site.

His Protein structure research includes elements of Biotin binding, GATAD2B, Helix-turn-helix, Protein folding and Biotin. His research in Repressor intersects with topics in Bacteriophage, Dimer, Activator and DNA-binding protein. His work deals with themes such as Enterococcus faecalis and Pheromone binding, Gene, Transcription factor, which intersect with DNA.

His most cited work include:

• Structural origins of high-affinity biotin binding to streptavidin. (868 citations)
• The use of an imaging proportional counter in macromolecular crystallography (464 citations)
• Structure of the cro repressor from bacteriophage λ and its interaction with DNA (455 citations)

What are the main themes of his work throughout his whole career to date?

His primary areas of study are Stereochemistry, Dioxygenase, Biochemistry, Crystal structure and Microbiology. His Stereochemistry study combines topics from a wide range of disciplines, such as Crystallography, Oxidoreductase, Ligand, Active site and Molecule. His work on Catechol dioxygenase as part of general Dioxygenase research is often related to Hydroxybenzoate, thus linking different fields of science.

His is doing research in Protein structure, DNA, Repressor, Gene and Protease, both of which are found in Biochemistry. His work carried out in the field of Protein structure brings together such families of science as Amino acid and Peptide sequence. His research integrates issues of Streptococcus, Mutant and Toxic shock syndrome, Staphylococcus aureus in his study of Microbiology.

He most often published in these fields:

• Stereochemistry (41.84%)
• Dioxygenase (27.66%)
• Biochemistry (22.70%)

What were the highlights of his more recent work (between 2004-2011)?

• Stereochemistry (41.84%)
• Dioxygenase (27.66%)
• Crystal structure (19.86%)

In recent papers he was focusing on the following fields of study:

Douglas H. Ohlendorf mainly focuses on Stereochemistry, Dioxygenase, Crystal structure, Biochemistry and Mutant. His Stereochemistry study incorporates themes from Oxidoreductase and Catechol. In his papers, Douglas H. Ohlendorf integrates diverse fields, such as Dioxygenase and Acinetobacter sp. ADP1.

His work on Plasma protein binding, Integrin, Protease and Fatty acid-binding protein as part of his general Biochemistry study is frequently connected to Fibronectin, thereby bridging the divide between different branches of science. Douglas H. Ohlendorf has included themes like Protein structure, Peptide sequence and C-terminus in his Protease study. His Mutant research is multidisciplinary, relying on both Endocrinology, Crystallography, Hydrolase, Dwarfism and Substrate.

Between 2004 and 2011, his most popular works were:

• Beta toxin catalyzes formation of nucleoprotein matrix in staphylococcal biofilms (127 citations)
• Structure of peptide sex pheromone receptor PrgX and PrgX/pheromone complexes and regulation of conjugation in Enterococcus faecalis. (112 citations)
• Structure and Biological Activities of Beta Toxin from Staphylococcus aureus (103 citations)

In his most recent research, the most cited papers focused on:

• Enzyme
• Gene
• DNA

The scientist’s investigation covers issues in Biochemistry, Plasma protein binding, Gene, Plasmid and Virulence. His Biochemistry study frequently draws connections to other fields, such as Microbiology. In the field of Microbiology, his study on Toxin overlaps with subjects such as Listeria ivanovii.

His Virulence research is multidisciplinary, incorporating elements of Biofilm, Bacteria and Nucleoprotein. In his study, Peptide sequence is inextricably linked to C5a peptidase, which falls within the broad field of Protein structure. Douglas H. Ohlendorf has researched Pheromone binding in several fields, including Enterococcus faecalis, Transcription factor, Genetic transfer and DNA.