His primary areas of study are Nuclear magnetic resonance spectroscopy, Biophysics, Stereochemistry, Crystallography and Protein structure. His biological study spans a wide range of topics, including Molecule, Pulse sequence and Analytical chemistry. The various areas that he examines in his Biophysics study include Biochemistry, Protein filament, Protein secondary structure, Alpha-synuclein and Microtubule.
His Stereochemistry research includes themes of Tubulin, Synucleinopathies and Binding selectivity. His work is dedicated to discovering how Crystallography, Ligand are connected with Two-component regulatory system, Kinase and Extracellular and other disciplines. His Protein structure study combines topics from a wide range of disciplines, such as Tau protein, Protein folding, Peptide sequence, Lanthanide and Monomer.
Christian Griesinger mostly deals with Nuclear magnetic resonance spectroscopy, Stereochemistry, Crystallography, Biophysics and Nuclear magnetic resonance. In his research, Chemical physics is intimately related to Molecule, which falls under the overarching field of Nuclear magnetic resonance spectroscopy. His study looks at the relationship between Crystallography and fields such as Protein structure, as well as how they intersect with chemical problems.
His work carried out in the field of Biophysics brings together such families of science as Membrane, Biochemistry and Alpha-synuclein. His Nuclear magnetic resonance research incorporates elements of Dipole and Molecular physics. Christian Griesinger combines subjects such as Computational chemistry and Residual with his study of Residual dipolar coupling.
His primary scientific interests are in Biophysics, Nuclear magnetic resonance spectroscopy, Crystallography, Alpha-synuclein and Membrane. Christian Griesinger has researched Biophysics in several fields, including Protein structure, Membrane protein, Small molecule and Amyloid. His study in Protein structure is interdisciplinary in nature, drawing from both Macromolecule and Fluorescence.
Nuclear magnetic resonance spectroscopy is the subject of his research, which falls under Nuclear magnetic resonance. His study in the field of Helix is also linked to topics like Population. His studies in Alpha-synuclein integrate themes in fields like Programmed cell death, Parkinsonism and Cell biology.
Nuclear magnetic resonance spectroscopy, Biophysics, Neuroscience, Chemical physics and Stereochemistry are his primary areas of study. His Nuclear magnetic resonance spectroscopy study is concerned with the larger field of Nuclear magnetic resonance. His Biophysics research is multidisciplinary, incorporating perspectives in Membrane, Membrane protein, Inner mitochondrial membrane and Cardiolipin.
Christian Griesinger interconnects Protein structure and Crystallography in the investigation of issues within Membrane protein. His research in Chemical physics intersects with topics in Microsecond, Dipole and Molecule. The Stereochemistry study combines topics in areas such as Polyketide and Binding site.
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Heteronuclear multidimensional NMR experiments for the structure determination of proteins in solution employing pulsed field gradients
Michael Sattler;Jürgen Schleucher;Christian Griesinger.
Progress in Nuclear Magnetic Resonance Spectroscopy (1999)
Clean TOCSY for proton spin system identification in macromolecules
C. Griesinger;G. Otting;K. Wuethrich;Richard R. Ernst.
Journal of the American Chemical Society (1988)
A general enhancement scheme in heteronuclear multidimensional NMR employing pulsed field gradients.
J. Schleucher;M. Schwendinger;M. Sattler;P. Schmidt.
Journal of Biomolecular NMR (1994)
Release of long-range tertiary interactions potentiates aggregation of natively unstructured α-synuclein
Carlos W. Bertoncini;Young-Sang Jung;Claudio O. Fernandez;Wolfgang Hoyer.
Proceedings of the National Academy of Sciences of the United States of America (2005)
Structural Polymorphism of 441-Residue Tau at Single Residue Resolution
Marco D Mukrasch;Stefan Bibow;Jegannath Korukottu;Sadasivam Jeganathan.
PLOS Biology (2009)
Pre‐fibrillar α‐synuclein variants with impaired β‐structure increase neurotoxicity in Parkinson's disease models
Damla Pinar Karpinar;Madhu Babu Gajula Balija;Sebastian Kügler;Felipe Opazo.
The EMBO Journal (2009)
Structural characterization of copper(II) binding to α-synuclein: Insights into the bioinorganic chemistry of Parkinson's disease
Rodolfo M. Rasia;Carlos W. Bertoncini;Derek Marsh;Wolfgang Hoyer.
Proceedings of the National Academy of Sciences of the United States of America (2005)
Direct measurement of angles between bond vectors in high-resolution NMR.
Bernd Reif;Mirko Hennig;Christian Griesinger.
Science (1997)
Atomic model of the type III secretion system needle
Antoine Loquet;Nikolaos G. Sgourakis;Rashmi Gupta;Karin Giller.
Nature (2012)
Oligodendroglial NMDA receptors regulate glucose import and axonal energy metabolism.
Aiman S. Saab;Iva D. Tzvetavona;Andrea Trevisiol;Selva Baltan.
Neuron (2016)
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