1986 - Fellow of John Simon Guggenheim Memorial Foundation
1985 - Fellow of the American Association for the Advancement of Science (AAAS)
His primary scientific interests are in Biochemistry, Bacteriophage, Mutant, Gene and Crystallography. The study of Biochemistry is intertwined with the study of Biophysics in a number of ways. His Bacteriophage study combines topics in areas such as Cyanophage, Genome, DNA, Prochlorococcus and Binding site.
In Mutant, Jonathan King works on issues like Viral Tail Proteins, which are connected to Thermolabile, Protein maturation, Immunoprecipitation, Trypsin and Glycoside hydrolase. The various areas that he examines in his Gene study include In vitro and Cell biology. His Crystallography research is multidisciplinary, relying on both Alanine and Viral capsid assembly, Capsid.
His primary areas of investigation include Biochemistry, Biophysics, Mutant, Protein folding and Crystallin. His work on Biochemistry deals in particular with Folding, Protein structure, In vitro, Amino acid and Denaturation. Jonathan King has included themes like Capsid and Monomer in his Biophysics study.
The study incorporates disciplines such as Mutation, Molecular biology and Cell biology in addition to Mutant. His Protein folding research integrates issues from Native state, Crystallography, Circular dichroism and Protein subunit. In his research, Fluorescence is intimately related to Tryptophan, which falls under the overarching field of Crystallin.
Jonathan King mostly deals with Crystallin, Biophysics, Biochemistry, Protein folding and Mutant. His Crystallin research includes elements of Protein aggregation, Tryptophan, Crystallography, Native state and Chaperone. His work deals with themes such as Mutation, Virus, Oxidative damage and Electron microscope, which intersect with Biophysics.
As part of his studies on Biochemistry, Jonathan King often connects relevant subjects like Monomer. His study in Protein folding is interdisciplinary in nature, drawing from both Lens protein, Lens, Protein subunit and Chemical stability. His research in Mutant intersects with topics in In vitro and Subunit interaction.
Jonathan King mainly focuses on Protein folding, Crystallin, Biochemistry, Chaperone and Protein aggregation. The Protein folding study combines topics in areas such as Mutant and Protein–protein interaction. His work investigates the relationship between Crystallin and topics such as Tryptophan that intersect with problems in In vitro, Recombinant DNA, Wild type, Lens and Tyrosine.
Carboxysome and Thylakoid are the primary areas of interest in his Biochemistry study. In his study, Amino acid, Metabolic pathway and Protein polymerization is strongly linked to Native state, which falls under the umbrella field of Chaperone. His studies deal with areas such as Crystallography and Biophysics as well as Protein aggregation.
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An unstable triplet repeat in a gene related to myotonic muscular dystrophy.
Y. H. Fu;A. Pizzuti;R. G. Fenwick;J. King.
Polypeptides of the tail fibres of bacteriophage T4
Jonathan King;Ulrich K. Laemmli.
Journal of Molecular Biology (1971)
Protein folding intermediates and inclusion body formation
Anna Mitraki;Jonathan King.
Nature Biotechnology (1989)
Protein misfolding and aggregation in cataract disease and prospects for prevention
Kate L. Moreau;Jonathan A. King.
Trends in Molecular Medicine (2012)
Specific aggregation of partially folded polypeptide chains: The molecular basis of inclusion body composition
Margaret A. Speed;Daniel I. C. Wang;Jonathan King.
Nature Biotechnology (1996)
Cyanobacterial photosynthesis in the oceans: the origins and significance of divergent light-harvesting strategies
Claire S. Ting;Gabrielle Rocap;Jonathan King;Sallie W. Chisholm;Sallie W. Chisholm.
Trends in Microbiology (2002)
Mechanism of head assembly and DNA encapsulation in Salmonella phage P22: I. Genes, proteins, structures and DNA maturation
David Botstein;Carol H. Waddell;Jonathan King.
Journal of Molecular Biology (1973)
Assembly of the tau of bacteriophage T4
Journal of Molecular Biology (1968)
Structure of epsilon15 bacteriophage reveals genome organization and DNA packaging/injection apparatus
Wen Jiang;Juan Chang;Joanita Jakana;Peter Weigele.
Nucleation and growth phases in the polymerization of coat and scaffolding subunits into icosahedral procapsid shells
P.E. Prevelige;D. Thomas;J. King.
Biophysical Journal (1993)
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