Thomas Szyperski spends much of his time researching Biochemistry, Protein structure, Nuclear magnetic resonance spectroscopy, Crystallography and Chemical shift. His research is interdisciplinary, bridging the disciplines of Stereochemistry and Biochemistry. Thomas Szyperski is involved in the study of Protein structure that focuses on Structural genomics in particular.
His study in Nuclear magnetic resonance spectroscopy is interdisciplinary in nature, drawing from both Two-dimensional nuclear magnetic resonance spectroscopy, Protein dynamics, Biological system, Analytical chemistry and Resonance. Thomas Szyperski has included themes like Conformational isomerism, Protein secondary structure and Protein folding in his Crystallography study. His Chemical shift research incorporates themes from Transverse relaxation-optimized spectroscopy and Protein structure prediction.
Thomas Szyperski focuses on Structural genomics, Computational biology, Biochemistry, Stereochemistry and Crystallography. His Structural genomics research entails a greater understanding of Protein structure. His Protein structure research incorporates elements of Peptide sequence, Sequence alignment and Protein folding.
His work on Citric acid cycle, Metabolism, Amino acid and Escherichia coli as part of his general Biochemistry study is frequently connected to Bacillus subtilis, thereby bridging the divide between different branches of science. His Crystallography study frequently draws parallels with other fields, such as Nuclear magnetic resonance spectroscopy. Within one scientific family, Thomas Szyperski focuses on topics pertaining to Analytical chemistry under Nuclear magnetic resonance spectroscopy, and may sometimes address concerns connected to Chemical shift.
His scientific interests lie mostly in Structural genomics, Computational biology, Protein structure, Crystallography and Biochemistry. Thomas Szyperski has researched Structural genomics in several fields, including Genetics and Protein domain. His biological study spans a wide range of topics, including Sequence, Protein folding, Peptide sequence, Biological system and Homology.
Crystallography is closely attributed to Nuclear magnetic resonance spectroscopy in his study. The various areas that Thomas Szyperski examines in his Nuclear magnetic resonance spectroscopy study include Supramolecular chemistry and Dipole. His study in the field of Binding site and Succinate dehydrogenase also crosses realms of Bacillus subtilis.
His primary areas of investigation include Protein structure, Crystallography, Nuclear magnetic resonance spectroscopy, Protein engineering and Biological system. His Protein design and Structural genomics investigations are all subjects of Protein structure research. Thomas Szyperski works mostly in the field of Structural genomics, limiting it down to topics relating to Molecular replacement and, in certain cases, Two-dimensional nuclear magnetic resonance spectroscopy.
His Crystallography study incorporates themes from Oligomer, Molecule, Stacking and Tetramer. His Nuclear magnetic resonance spectroscopy research includes themes of Analytical chemistry, Kinetic isotope effect and Carbon-13 NMR. His Protein engineering study integrates concerns from other disciplines, such as Peptide sequence and Crystal structure.
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Consistent blind protein structure generation from NMR chemical shift data
Yang Shen;Oliver Lange;Frank Delaglio;Paolo Rossi.
Proceedings of the National Academy of Sciences of the United States of America (2008)
Stereospecific nuclear magnetic resonance assignments of the methyl groups of valine and leucine in the DNA-binding domain of the 434 repressor by biosynthetically directed fractional 13C labeling.
Dario Neri;Thomas Szyperski;Gottfried Otting;Hans Senn.
Biosynthetically directed fractional 13C-labeling of proteinogenic amino acids. An efficient analytical tool to investigate intermediary metabolism.
FEBS Journal (1995)
GFT NMR, a new approach to rapidly obtain precise high-dimensional NMR spectral information
Seho Kim;Thomas Szyperski.
Journal of the American Chemical Society (2003)
Biosynthetically Directed Fractional 13C-labeling of Proteinogenic Amino Acids
FEBS Journal (1995)
Metabolic flux ratio analysis of genetic and environmental modulations of Escherichia coli central carbon metabolism.
Uwe Sauer;Daniel R. Lasko;Jocelyne Fiaux;Michel Hochuli.
Journal of Bacteriology (1999)
NMR scalar couplings across Watson-Crick base pair hydrogen bonds in DNA observed by transverse relaxation-optimized spectroscopy
Konstantin Pervushin;Akira Ono;César Fernández;Thomas Szyperski.
Proceedings of the National Academy of Sciences of the United States of America (1998)
Metabolic Flux Responses to Pyruvate Kinase Knockout in Escherichia coli
Marcel Emmerling;Michael Dauner;Aaron Ponti;Jocelyne Fiaux.
Journal of Bacteriology (2002)
Metabolic fluxes in riboflavin-producing Bacillus subtilis
Uwe Sauer;Vassily Hatzimanikatis;James E. Bailey;Michel Hochuli.
Nature Biotechnology (1997)
13C-NMR, MS and metabolic flux balancing in biotechnology research.
Quarterly Reviews of Biophysics (1998)
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