H. Jane Dyson mainly focuses on Protein folding, Crystallography, Protein structure, Biophysics and Intrinsically disordered proteins. His research in Protein folding intersects with topics in Peptide Conformation, Function, Folding, Stereochemistry and Computational biology. The various areas that H. Jane Dyson examines in his Crystallography study include Sulfur, Protein secondary structure and Chemical shift.
His Protein structure research is multidisciplinary, incorporating elements of Genetics, Catalytic cycle, Dihydrofolate reductase and Active site. His Biophysics study combines topics in areas such as Plasma protein binding, Biochemistry, Binding site and CREB-binding protein. His biological study spans a wide range of topics, including Class, Conformational ensembles and Cell biology.
His main research concerns Crystallography, Protein structure, Protein folding, Biophysics and Biochemistry. His studies in Crystallography integrate themes in fields like Folding, Nuclear magnetic resonance spectroscopy and Protein secondary structure. In his study, which falls under the umbrella issue of Protein secondary structure, Chemical physics is strongly linked to Chemical shift.
His study in Protein structure is interdisciplinary in nature, drawing from both Plasma protein binding, Stereochemistry, Dihydrofolate reductase and Ternary complex. H. Jane Dyson works mostly in the field of Protein folding, limiting it down to topics relating to Intrinsically disordered proteins and, in certain cases, Computational biology. His Biophysics study incorporates themes from Transcription factor, Transactivation, CREB-binding protein, Isothermal titration calorimetry and Binding site.
His primary areas of investigation include DNA, Biophysics, Computational biology, Binding site and Zinc finger. His DNA research includes themes of RNA, Transcription factor, Gene, Chaperone and Nuclear magnetic resonance spectroscopy. He has researched Biophysics in several fields, including A-site, Tetramer, Allosteric regulation and Transactivation.
His Computational biology research includes elements of Cell cycle, Cell and Intrinsically disordered proteins. His work focuses on many connections between Intrinsically disordered proteins and other disciplines, such as Characterization, that overlap with his field of interest in Electron paramagnetic resonance, Protein folding and Conformational ensembles. His research is interdisciplinary, bridging the disciplines of CREB-binding protein and Binding site.
H. Jane Dyson mostly deals with Biophysics, Computational biology, Intrinsically disordered proteins, Allosteric regulation and Tetramer. His Biophysics study combines topics from a wide range of disciplines, such as Ternary complex, Spin relaxation, Mutant and Transactivation. The Computational biology study combines topics in areas such as Cell and Cell cycle.
His research integrates issues of Characterization, Conformational ensembles, Function and Protein folding in his study of Intrinsically disordered proteins. H. Jane Dyson combines subjects such as Cellular Regulation, Posttranslational modification, Globular protein and Protein–protein interaction with his study of Allosteric regulation. H. Jane Dyson interconnects Hydrophobic effect, Transcription factor and Protomer in the investigation of issues within Tetramer.
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Intrinsically unstructured proteins: re-assessing the protein structure-function paradigm.
Peter E Wright;H.Jane Dyson.
Journal of Molecular Biology (1999)
Coupling of folding and binding for unstructured proteins
H.Jane Dyson;Peter E Wright.
Current Opinion in Structural Biology (2002)
Intrinsically disordered proteins in cellular signalling and regulation.
Peter E. Wright;H. Jane Dyson.
Nature Reviews Molecular Cell Biology (2015)
Mechanism of coupled folding and binding of an intrinsically disordered protein
Kenji Sugase;H. Jane Dyson;Peter E. Wright.
Linking Folding and Binding
Peter E Wright;H Jane Dyson.
Current Opinion in Structural Biology (2009)
The Dynamic Energy Landscape of Dihydrofolate Reductase Catalysis
David D. Boehr;Dan McElheny;H. Jane Dyson;Peter E. Wright.
Solution structure of the KIX domain of CBP bound to the transactivation domain of CREB: a model for activator:coactivator interactions.
Ishwar Radhakrishnan;Gabriela C Pérez-Alvarado;David Parker;H.Jane Dyson.
COPPER BINDING TO THE PRION PROTEIN : STRUCTURAL IMPLICATIONS OF FOUR IDENTICAL COOPERATIVE BINDING SITES
John H. Viles;Fred E. Cohen;Stanley B. Prusiner;David B. Goodin.
Proceedings of the National Academy of Sciences of the United States of America (1999)
Folding of peptide fragments comprising the complete sequence of proteins. Models for initiation of protein folding. II. Plastocyanin.
H.Jane Dyson;James R. Sayre;Gene Merutka;Hang-Cheol Shin.
Journal of Molecular Biology (1992)
‘Random coil’ 1H chemical shifts obtained as a function of temperature and trifluoroethanol concentration for the peptide series GGXGG
Gene Merutka;H. Jane Dyson;Peter E. Wright.
Journal of Biomolecular NMR (1995)
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