His main research concerns Myoglobin, Stereochemistry, Heme, Histidine and Ligand. His Myoglobin research is multidisciplinary, relying on both Crystallography, Hemin, Ligand, Hydrogen bond and Hemeprotein. John S. Olson integrates many fields in his works, including Stereochemistry and Side chain.
The various areas that he examines in his Heme study include Hemoglobin, Reaction rate constant and Carbon monoxide. His research in Histidine tackles topics such as Oxygen binding which are related to areas like Hydrogen peroxide and Peroxide. The Ligand study combines topics in areas such as Amino acid, Ligand binding assay, Molecular dynamics, Steric effects and Binding site.
John S. Olson spends much of his time researching Stereochemistry, Heme, Hemoglobin, Myoglobin and Biochemistry. His Stereochemistry research is multidisciplinary, incorporating elements of Reaction rate constant, Histidine, Hydrogen bond and Ligand. John S. Olson has researched Heme in several fields, including Carbon monoxide, Plasma protein binding and Binding site.
His research investigates the connection with Hemoglobin and areas like Oxygen which intersect with concerns in Analytical chemistry. The study incorporates disciplines such as Crystallography, Steric effects, Ligand and Hemeprotein in addition to Myoglobin. His study on Mutant, Recombinant DNA and Escherichia coli is often connected to Cerebratulus lacteus as part of broader study in Biochemistry.
John S. Olson mainly investigates Hemoglobin, Heme, Stereochemistry, Biochemistry and Hemin. His studies deal with areas such as Ferric, Biophysics, Protein subunit and Plasma protein binding as well as Hemoglobin. His work carried out in the field of Heme brings together such families of science as Myoglobin, Recombinant DNA, Autoxidation, Methemoglobin and Globin.
John S. Olson merges many fields, such as Myoglobin and Side chain, in his writings. John S. Olson interconnects Oxygen binding, Ligand, Protein structure, Redox and Binding site in the investigation of issues within Stereochemistry. In general Biochemistry, his work in Mutant, Escherichia coli, Methionine and Extracellular is often linked to Platelet adhesiveness linking many areas of study.
His primary areas of investigation include Stereochemistry, Heme, Hemoglobin, Oxygen binding and Ligand. His Stereochemistry research incorporates elements of Hemeprotein and Binding site. His Heme research is mostly focused on the topic Hemin.
His Hemoglobin study introduces a deeper knowledge of Biochemistry. His work deals with themes such as Protein structure, Ligand and Ligand Binding Protein, which intersect with Oxygen binding. His study in Ligand is interdisciplinary in nature, drawing from both Active site, Myoglobin and Histidine.
This overview was generated by a machine learning system which analysed the scientist’s body of work. If you have any feedback, you can contact us here.
Watching a Protein as it Functions with 150-ps Time-Resolved X-ray Crystallography
Friedrich Schotte;Manho Lim;Timothy Albert Jackson;Aleksandr V. Smirnov.
Mechanisms of Ligand Recognition in Myoglobin
Barry A. Springer;Stephen G. Sligar;John S. Olson;George N. Jr. Phillips.
Chemical Reviews (1994)
Mechanism of NO-Induced Oxidation of Myoglobin and Hemoglobin†
Raymund F. Eich;Tiansheng Li;Douglas D. Lemon;Daniel H. Doherty.
Rate of reaction with nitric oxide determines the hypertensive effect of cell-free hemoglobin
Daniel H. Doherty;Michael P. Doyle;Shawn R. Curry;Rita J. Vali.
Nature Biotechnology (1998)
The mechanism of autooxidation of myoglobin.
R E Brantley;S J Smerdon;A J Wilkinson;E W Singleton.
Journal of Biological Chemistry (1993)
High-resolution crystal structures of distal histidine mutants of sperm whale myoglobin.
Michael L. Quillin;Robert M. Arduini;John S. Olson;George N. Phillips.
Journal of Molecular Biology (1994)
Structural Determinants of the Stretching Frequency of CO Bound to Myoglobin
Tiansheng Li;Michael L. Quillin;George N. Phillips;John S. Olson.
The Mechanism of Action of Xanthine Oxidase
John S. Olson;David P. Ballou;Graham Palmer;Vincent Massey.
Journal of Biological Chemistry (1974)
Mapping the pathways for O2 entry into and exit from myoglobin.
Emily E. Scott;Quentin H. Gibson;John S. Olson.
Journal of Biological Chemistry (2001)
Kinetic Pathways and Barriers for Ligand Binding to Myoglobin
John S. Olson;George N. Phillips.
Journal of Biological Chemistry (1996)
If you think any of the details on this page are incorrect, let us know.
We appreciate your kind effort to assist us to improve this page, it would be helpful providing us with as much detail as possible in the text box below: