Hans Robert Kalbitzer mostly deals with Biochemistry, Nuclear magnetic resonance spectroscopy, Stereochemistry, Protein structure and GTPase. His Biochemistry study which covers Biophysics that intersects with Cytoplasm. Nuclear magnetic resonance spectroscopy is a subfield of Nuclear magnetic resonance that Hans Robert Kalbitzer explores.
His Stereochemistry study combines topics from a wide range of disciplines, such as Active site, Signal transduction and Effector. His work carried out in the field of Protein structure brings together such families of science as Crystallography, Residual, Binding site and Standard deviation. His research in GTPase intersects with topics in Glutamine, GTP', Mutant and Deamidation.
Hans Robert Kalbitzer mainly focuses on Nuclear magnetic resonance spectroscopy, Biochemistry, Crystallography, Stereochemistry and Nuclear magnetic resonance. Hans Robert Kalbitzer interconnects Proton NMR, NMR spectra database, Analytical chemistry, Protein structure and Chemical shift in the investigation of issues within Nuclear magnetic resonance spectroscopy. Many of his studies on Biochemistry involve topics that are commonly interrelated, such as Biophysics.
His Crystallography research is multidisciplinary, incorporating perspectives in Electron paramagnetic resonance, Molecule and Metal. His work in Stereochemistry covers topics such as GTP' which are related to areas like Guanine. His Nuclear magnetic resonance research is mostly focused on the topic Two-dimensional nuclear magnetic resonance spectroscopy.
Hans Robert Kalbitzer mainly investigates Nuclear magnetic resonance spectroscopy, Chemical shift, Crystallography, Stereochemistry and Biochemistry. His Nuclear magnetic resonance spectroscopy study combines topics in areas such as Amino acid, Protein structure, Guanine and Analytical chemistry. His study on Chemical shift also encompasses disciplines like
In his study, Polymer is strongly linked to Molecule, which falls under the umbrella field of Crystallography. His work in Stereochemistry addresses subjects such as Side chain, which are connected to disciplines such as Asparagine. His Biochemistry study frequently intersects with other fields, such as Biophysics.
The scientist’s investigation covers issues in Nuclear magnetic resonance spectroscopy, Stereochemistry, Biochemistry, Signal transduction and Chemical shift. Hans Robert Kalbitzer has researched Nuclear magnetic resonance spectroscopy in several fields, including Protein structure, Volume and Analytical chemistry. His studies in Protein structure integrate themes in fields like Crystallography, Molecular physics, Two-dimensional nuclear magnetic resonance spectroscopy and Protein folding.
The study incorporates disciplines such as Dimer and Active site in addition to Stereochemistry. His research integrates issues of Biophysics and Endocrinology, Steatosis in his study of Biochemistry. The concepts of his Signal transduction study are interwoven with issues in Allosteric regulation, Cyclen and Effector.
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Dynamic properties of the Ras switch I region and its importance for binding to effectors.
Michael Spoerner;Christian Herrmann;Ingrid R. Vetter;Hans Robert Kalbitzer.
Proceedings of the National Academy of Sciences of the United States of America (2001)
Substrate-assisted catalysis as a mechanism for GTP hydrolysis of p21ras and other GTP-binding proteins.
Thomas Schweins;Matthias Geyer;Klaus Scheffzek;Arieh Warshel.
Nature Structural & Molecular Biology (1995)
Structure and function of bacterial cold shock proteins.
G. Horn;R. Hofweber;Werner Kremer;Hans Robert Kalbitzer.
Cellular and Molecular Life Sciences (2007)
Human immunodeficiency virus type 1 Nef protein is incorporated into virus particles and specifically cleaved by the viral proteinase
Reinhold Welker;Hubert Kottler;Hans Robert Kalbitzer;Hans-Georg Kräusslich.
Conformational transitions in p21ras and in its complexes with the effector protein Raf-RBD and the GTPase activating protein GAP.
Matthias Geyer;Thomas Schweins;Christian Herrmann;Thomas Prisner.
Combined chemical shift changes and amino acid specific chemical shift mapping of protein–protein interactions
Frank H. Schumann;Hubert Riepl;Till Maurer;Wolfram Gronwald.
Journal of Biomolecular NMR (2007)
Thermodynamic and kinetic characterization of the interaction between the Ras binding domain of AF6 and members of the Ras subfamily.
Thomas Linnemann;Matthias Geyer;Birgit K. Jaitner;Christoph Block.
Journal of Biological Chemistry (1999)
Structure of the Ras-binding domain of RalGEF and implications for Ras binding and signalling
Matthias Geyer;Christian Herrmann;Sabine Wohlgemuth;Alfred Wittinghofer.
Nature Structural & Molecular Biology (1997)
Distribution of chemical shifts in 1H nuclear magnetic resonance spectra of proteins
Karl-Heinz Groß;Hans Robert Kalbitzer.
Journal of Magnetic Resonance (1988)
Conformational states of human rat sarcoma (Ras) protein complexed with its natural ligand GTP and their role for effector interaction and GTP hydrolysis.
Michael Spoerner;Constantin Hozsa;Johann A. Poetzl;Kerstin Reiss.
Journal of Biological Chemistry (2010)
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