His primary areas of investigation include Biochemistry, Stereochemistry, Crystallography, Glutamate dehydrogenase and Enzyme. His NAD+ kinase, Oxidoreductase, Escherichia coli and Clostridium symbiosum study in the realm of Biochemistry interacts with subjects such as Enoyl-acyl carrier protein reductase. His research in Stereochemistry intersects with topics in Residue, Crystal structure, Cofactor and Binding site.
His Crystallography research is multidisciplinary, incorporating elements of Protein structure, Ferritin, Molecule and Recombinant DNA. His work deals with themes such as Amino acid and Pyrococcus furiosus, which intersect with Glutamate dehydrogenase. His specific area of interest is Enzyme, where David W. Rice studies Phosphofructokinase 2.
His scientific interests lie mostly in Biochemistry, Stereochemistry, Enzyme, Crystallography and Glutamate dehydrogenase. His Biochemistry research focuses on Escherichia coli, Reductase, Protein structure, Oxidoreductase and Peptide sequence. His work in Stereochemistry addresses subjects such as Active site, which are connected to disciplines such as Binding site and Lyase.
His Enzyme research incorporates elements of Pyrococcus furiosus, Protein subunit and Toxoplasma gondii. The Crystallography study combines topics in areas such as Crystallization and Dimer. David W. Rice combines subjects such as Thermotoga maritima, Mutant and Thermostability with his study of Glutamate dehydrogenase.
David W. Rice focuses on Biochemistry, Enzyme, Toxoplasma gondii, Escherichia coli and Stereochemistry. He brings together Biochemistry and Enoyl-acyl carrier protein reductase to produce work in his papers. His work on Reductase, Histidine and Cutinase as part of his general Enzyme study is frequently connected to Metastasis and Asparagine synthetase, thereby bridging the divide between different branches of science.
The various areas that David W. Rice examines in his Reductase study include Oxidoreductase, Structure–activity relationship and NAD+ kinase. His work deals with themes such as Crystallography and Burkholderia pseudomallei, which intersect with Escherichia coli. Within one scientific family, David W. Rice focuses on topics pertaining to Active site under Stereochemistry, and may sometimes address concerns connected to Lyase, Binding site, Conformational change, Catalytic cycle and Substrate.
The scientist’s investigation covers issues in Active site, Stereochemistry, Toxoplasma gondii, Microbiology and Biochemistry. His study in Active site is interdisciplinary in nature, drawing from both Catalytic cycle, Conformational change, Substrate and Binding site. David W. Rice has included themes like Crystallography, Peptide sequence, Phosphoglycerate kinase and Ternary complex in his Conformational change study.
David W. Rice undertakes multidisciplinary investigations into Stereochemistry and Oxygen binding in his work. His Microbiology research is multidisciplinary, incorporating elements of Enterobacteriaceae, Antibacterial agent, eIF4A and Translation factor. His Biochemistry research includes elements of Acanthamoeba castellanii and Drug resistance.
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Structure of human lactoferrin: Crystallographic structure analysis and refinement at 2·8 Å resolution
Bryan F. Anderson;Heather M. Baker;Gillian E. Norris;David W. Rice.
Journal of Molecular Biology (1989)
Ferritin: Design and Formation of an Iron-Storage Molecule
G. C. Ford;Pauline May Harrison;D. W. Rice;J. M. A. Smith.
Philosophical Transactions of the Royal Society B (1984)
Molecular basis of triclosan activity
Colin W. Levy;Anna Roujeinikova;Svetlana Sedelnikova;Patrick J. Baker.
The structure of Pyrococcus furiosus glutamate dehydrogenase reveals a key role for ion-pair networks in maintaining enzyme stability at extreme temperatures
K. S. P. Yip;T. J. Stillman;K. L. Britton;P. J. Artymiuk.
Sequence, structure and activity of phosphoglycerate kinase: a possible hinge-bending enzyme.
R. D. Banks;C. C. F. Blake;P. R. Evans;P. R. Evans;R. Haser;R. Haser.
An Inhibitor of Ftsz with Potent and Selective Anti-Staphylococcal Activity.
David J. Haydon;Neil R. Stokes;Rebecca Ure;Greta Galbraith.
Comparison of the three-dimensional structures of recombinant human H and horse L ferritins at high resolution.
Paul D Hempstead;Stephen J Yewdall;Alisdair R Fernie;David M Lawson.
Journal of Molecular Biology (1997)
Identification of tertiary structure resemblance in proteins using a maximal common subgraph isomorphism algorithm.
Helen M. Grindley;Peter J. Artymiuk;David W. Rice;Peter Willett.
Journal of Molecular Biology (1993)
Fatty acid and sterol metabolism: potential antimicrobial targets in apicomplexan and trypanosomatid parasitic protozoa
C.W. Roberts;R. McLeod;D.W. Rice;Michael L. Ginger.
Molecular and Biochemical Parasitology (2003)
Protein thermostability above 100°C: A key role for ionic interactions
Costantino Vetriani;Dennis L. Maeder;Nicola Tolliday;Kitty S.-P. Yip.
Proceedings of the National Academy of Sciences of the United States of America (1998)
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