What is he best known for?
The fields of study he is best known for:
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.
His most cited work include:
- Dynamic properties of the Ras switch I region and its importance for binding to effectors (229 citations)
- Substrate-assisted catalysis as a mechanism for GTP hydrolysis of p21ras and other GTP-binding proteins. (214 citations)
- Conformational transitions in p21ras and in its complexes with the effector protein Raf-RBD and the GTPase activating protein GAP (184 citations)
What are the main themes of his work throughout his whole career to date?
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.
He most often published in these fields:
- Nuclear magnetic resonance spectroscopy (31.58%)
- Biochemistry (21.36%)
- Crystallography (18.58%)
What were the highlights of his more recent work (between 2009-2021)?
- Nuclear magnetic resonance spectroscopy (31.58%)
- Chemical shift (9.29%)
- Crystallography (18.58%)
In recent papers he was focusing on the following fields of study:
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
- Nucleotide which intersects with area such as GTP' and Proton NMR,
- Random coil which connect with Amide.
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.
Between 2009 and 2021, his most popular works were:
- Conformational states of human rat sarcoma (Ras) protein complexed with its natural ligand GTP and their role for effector interaction and GTP hydrolysis. (90 citations)
- Stabilizing a weak binding state for effectors in the human ras protein by cyclen complexes (84 citations)
- Metal–Bis(2‐picolyl)amine Complexes as State 1(T) Inhibitors of Activated Ras Protein (53 citations)
In his most recent research, the most cited papers focused on:
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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