2020 - Davy Medal, Royal Society of London (UK) for inventing powerful chemical methods that directly manipulate complex biological molecules, enabling elucidation and control of biological function and mechanism in vitro and in vivo, beyond the limits of genetics.
2017 - Member of Academia Europaea
2015 - Fellow of the Royal Society, United Kingdom
2005 - Corday–Morgan Prize, Royal Society of Chemistry (UK)
1999 - Meldola Medal and Prize, Royal Society of Chemistry (UK)
His main research concerns Biochemistry, Stereochemistry, Glycosylation, Organic chemistry and Glycoprotein. His research in Stereochemistry intersects with topics in Nucleophilic substitution, Reaction mechanism and Palladium. His research investigates the connection with Glycosylation and areas like Computational biology which intersect with concerns in Glycobiology and Protein folding.
His Organic chemistry research incorporates elements of Amino acid and Bioconjugation. His Glycoprotein research is multidisciplinary, incorporating perspectives in Immunoglobulin G and Antibody. The study incorporates disciplines such as Arabidopsis thaliana, Synthetic biology, Chemical modification, Combinatorial chemistry and Dehydroalanine in addition to Cysteine.
His primary areas of investigation include Stereochemistry, Biochemistry, Organic chemistry, Combinatorial chemistry and Glycosylation. The Stereochemistry study combines topics in areas such as Amino acid, Hydrogen bond, Subtilisin and Peptide. His research integrates issues of Serine protease and Chemical modification in his study of Subtilisin.
His Biochemistry research focuses on Enzyme, Glycan, Glycoconjugate, Glycoprotein and Cysteine. His study in Carbohydrate, Catalysis and Reagent is done as part of Organic chemistry. Combinatorial chemistry and Dehydroalanine are commonly linked in his work.
Benjamin G. Davis focuses on Biochemistry, Stereochemistry, Combinatorial chemistry, Dehydroalanine and Nanotechnology. Biophysics is closely connected to In vivo in his research, which is encompassed under the umbrella topic of Biochemistry. He combines subjects such as Amino acid, Conformational isomerism, Nucleophile and Hydrogen bond with his study of Stereochemistry.
Benjamin G. Davis works mostly in the field of Amino acid, limiting it down to topics relating to Residue and, in certain cases, Formylation, Reactivity and Cysteine. His work carried out in the field of Dehydroalanine brings together such families of science as Enzyme, Small molecule, Side chain, Kinase and Binding site. His Glycosylation research is multidisciplinary, incorporating elements of Congenital myasthenic syndrome, Antibiotics, Glycan and Nucleoside.
His primary scientific interests are in Combinatorial chemistry, Biochemistry, Residue, Nanotechnology and Amino acid. His Combinatorial chemistry research incorporates themes from Allyl Sulfide, Olefin fiber, Molecule, Selenide and Salt metathesis reaction. He has researched Biochemistry in several fields, including Ms analysis and Antibody.
The various areas that Benjamin G. Davis examines in his Residue study include Surface modification, Site selectivity, Metal, Trifluoromethyl and Trifluoromethanesulfonate. His Nanotechnology study incorporates themes from In vivo, Carbon, Micrometre and Biological effect. His studies in Amino acid integrate themes in fields like Sense Codon, Transfer RNA, Protein function and ENCODE.
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Glycoprotein synthesis: an update.
David P. Gamblin;Eoin M. Scanlan;Benjamin G. Davis.
Chemical Reviews (2009)
Selective chemical protein modification
Christopher D Spicer;Benjamin G Davis.
Nature Communications (2014)
Synthesis of glycoproteins.
Benjamin G. Davis.
Chemical Reviews (2002)
Lectins: tools for the molecular understanding of the glycocode
Moira Ambrosi;Neil R. Cameron;Benjamin G. Davis.
Organic and Biomolecular Chemistry (2005)
Chemical modification of proteins at cysteine: opportunities in chemistry and biology.
Justin M. Chalker;Gonçalo J. L. Bernardes;Yuya A. Lin;Benjamin G. Davis.
Chemistry-an Asian Journal (2009)
Functional divergence in the glutathione transferase superfamily in plants. Identification of two classes with putative functions in redox homeostasis in Arabidopsis thaliana.
David P. Dixon;Benjamin G. Davis;Robert Edwards.
Journal of Biological Chemistry (2002)
Structure of a flavonoid glucosyltransferase reveals the basis for plant natural product modification
Wendy Offen;Carlos Martinez-Fleites;Min Yang;Eng Kiat-Lim.
The EMBO Journal (2006)
Allyl Sulfides Are Privileged Substrates in Aqueous Cross-Metathesis: Application to Site-Selective Protein Modification
Yuya A. Lin;Justin M. Chalker;Nicola Floyd;Gonçalo J. L. Bernardes.
Journal of the American Chemical Society (2008)
Expanding the diversity of chemical protein modification allows post-translational mimicry
Sander I. van Kasteren;Holger B. Kramer;Henrik H. Jensen;Sandra J. Campbell.
Nature (2007)
Facile conversion of cysteine and alkyl cysteines to dehydroalanine on protein surfaces: versatile and switchable access to functionalized proteins.
Gonçalo J. L. Bernardes;Justin M. Chalker;James C. Errey;Benjamin G. Davis.
Journal of the American Chemical Society (2008)
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