Biochemistry, Protein structure, Biophysics, Crystallography and Protein secondary structure are his primary areas of study. His Protein structure research is multidisciplinary, relying on both Plasma protein binding and Amyloid. His biological study spans a wide range of topics, including Cleavage, Serine, Target protein, Transmembrane protein and Protein folding.
His Crystallography research is multidisciplinary, incorporating perspectives in Intercalation, Dipole, Binding site and Thermodynamics. His Protein secondary structure study incorporates themes from Dihedral angle and Nuclear magnetic resonance spectroscopy. His biological study deals with issues like DNA-binding domain, which deal with fields such as Cysteine, Zinc finger and Nuclear Overhauser effect.
His primary areas of investigation include Biochemistry, Crystallography, Protein structure, Biophysics and DNA. When carried out as part of a general Biochemistry research project, his work on Peptide and Binding site is frequently linked to work in P3 peptide, therefore connecting diverse disciplines of study. His studies in Binding site integrate themes in fields like Zinc finger, Wild type, Cysteine, DNA-binding domain and Glucocorticoid receptor.
His work carried out in the field of Crystallography brings together such families of science as Nuclear magnetic resonance spectroscopy, Stereochemistry, Isothermal titration calorimetry and Protein secondary structure. Torleif Härd interconnects Ribosome, Ribosomal protein, Ribosomal RNA, Protein folding and Protein engineering in the investigation of issues within Protein structure. His research integrates issues of Plasma protein binding, Amyloid β and Dimer in his study of Biophysics.
His scientific interests lie mostly in Biophysics, Peptide, Biochemistry, Amyloid and Amyloid β. His study looks at the relationship between Biophysics and fields such as Plasma protein binding, as well as how they intersect with chemical problems. His Peptide research incorporates elements of Protein engineering and Protein aggregation.
His research in Protein aggregation intersects with topics in Dynamics, Crystallography, Solid-state nuclear magnetic resonance, Nuclear magnetic resonance and Magic angle spinning. His study in the fields of Intrinsically disordered proteins, Binding site and Binding protein under the domain of Biochemistry overlaps with other disciplines such as Complement system. His Amyloid research is multidisciplinary, incorporating elements of Eukaryotic organism and Protein folding.
His primary areas of study are Peptide, Biochemistry, Biophysics, Protein engineering and Amyloid. His Peptide research spans across into areas like Biochemistry of Alzheimer's disease and Barrel. Torleif Härd merges many fields, such as Biophysics and P3 peptide, in his writings.
His Protein engineering research incorporates themes from Amyloid beta, Protein aggregation and Rational design. His work deals with themes such as Binding protein, Apolipoprotein E, Plasma protein binding and Senile plaques, which intersect with Protein aggregation. The concepts of his Amyloid study are interwoven with issues in Intrinsically disordered proteins, Binding site, Protein–protein interaction and Protein folding.
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Solution structure of the glucocorticoid receptor DNA-binding domain
Torleif Härd;Edwin Kellenbach;Rolf Boelens;Bonnie A. Maler.
Rapid screening for improved solubility of small human proteins produced as fusion proteins in Escherichia coli
Martin Hammarström;Niklas Hellgren;Susanne van den Berg;Helena Berglund.
Protein Science (2009)
Stabilization of a β-hairpin in monomeric Alzheimer's amyloid-β peptide inhibits amyloid formation
Wolfgang Hoyer;Caroline Grönwall;Andreas Jonsson;Stefan Ståhl.
Proceedings of the National Academy of Sciences of the United States of America (2008)
Stabilization of neurotoxic Alzheimer amyloid-β oligomers by protein engineering
Anders Sandberg;Leila M. Luheshi;Sofia Söllvander;Teresa Pereira de Barros.
Proceedings of the National Academy of Sciences of the United States of America (2010)
Improved solubility of TEV protease by directed evolution.
Susanne van den Berg;Per-Åke Löfdahl;Torleif Härd;Helena Berglund.
Journal of Biotechnology (2006)
Inhibition of Amyloid Formation
Torleif Härd;Christofer Lendel.
Journal of Molecular Biology (2012)
Autoproteolysis coupled to protein folding in the SEA domain of the membrane-bound MUC1 mucin.
Bertil Macao;Denny G A Johansson;Gunnar C Hansson;Torleif Härd.
Nature Structural & Molecular Biology (2006)
Structural characterization of a minimal functional transactivation domain from the human glucocorticoid receptor.
Karin Dahlman-Wright;Herbert Baumann;Iain J. McEwan;Tova Almlof.
Proceedings of the National Academy of Sciences of the United States of America (1995)
Solution Structure and DNA-binding Properties of a Thermostable Protein From the Archaeon Sulfolobus Solfataricus
Herbert Baumann;Stefan Knapp;Thomas Lundbäck;Rudolf Ladenstein.
Nature Structural & Molecular Biology (1994)
His tag effect on solubility of human proteins produced in Escherichia coli: a comparison between four expression vectors
Esmeralda A. Woestenenk;Martin Hammarström;Susanne van den Berg;Torleif Härd.
Journal of Structural and Functional Genomics (2004)
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