What is she best known for?
The fields of study she is best known for:
Angela M. Gronenborn mainly investigates Crystallography, Nuclear magnetic resonance spectroscopy, Protein structure, Nuclear Overhauser effect and Nuclear magnetic resonance.
Her Crystallography research includes elements of Dihedral angle, Molecule, Hydrogen bond and Protein secondary structure.
Her Nuclear magnetic resonance spectroscopy research is classified as research in Stereochemistry.
Her study looks at the intersection of Protein structure and topics like Macromolecule with Residual dipolar coupling.
She combines subjects such as Molecular physics, Computational chemistry, Proton and A protein with her study of Nuclear Overhauser effect.
Her Nuclear magnetic resonance research integrates issues from Spectroscopy and NMR spectra database.
Her most cited work include:
- Solution structure of a calmodulin-target peptide complex by multidimensional NMR. (1135 citations)
- Deviations from the simple two-parameter model-free approach to the interpretation of nitrogen-15 nuclear magnetic relaxation of proteins (922 citations)
- Overcoming the overlap problem in the assignment of 1H NMR spectra of larger proteins by use of three-dimensional heteronuclear 1H-15N Hartmann-Hahn-multiple quantum coherence and nuclear Overhauser-multiple quantum coherence spectroscopy: application to interleukin 1 beta (775 citations)
What are the main themes of her work throughout her whole career to date?
Crystallography, Nuclear magnetic resonance spectroscopy, Stereochemistry, Protein structure and Biochemistry are her primary areas of study.
Angela M. Gronenborn interconnects Dihedral angle, Hydrogen bond and Dimer in the investigation of issues within Crystallography.
Her Nuclear magnetic resonance spectroscopy research is multidisciplinary, incorporating elements of Molecule and Protein secondary structure.
Her work in the fields of Stereochemistry, such as Proton NMR, overlaps with other areas such as Side chain.
Her Protein structure research is multidisciplinary, relying on both Molecular physics, Peptide sequence and Protein folding.
Her Nuclear magnetic resonance research incorporates themes from Spectral line, Spectroscopy, Resonance and Homonuclear molecule.
She most often published in these fields:
- Crystallography (32.22%)
- Nuclear magnetic resonance spectroscopy (28.23%)
- Stereochemistry (24.40%)
What were the highlights of her more recent work (between 2009-2021)?
- Biochemistry (20.57%)
- Protein structure (23.60%)
- Nuclear magnetic resonance spectroscopy (28.23%)
In recent papers she was focusing on the following fields of study:
Her main research concerns Biochemistry, Protein structure, Nuclear magnetic resonance spectroscopy, Crystallography and Magic angle spinning.
Her research in Biochemistry tackles topics such as Stereochemistry which are related to areas like Amino acid.
The study incorporates disciplines such as Molecular biology, Peptide sequence, Protein subunit and Protein domain in addition to Protein structure.
Her study focuses on the intersection of Nuclear magnetic resonance spectroscopy and fields such as Molecular dynamics with connections in the field of Chemical physics.
Her study in Crystallography is interdisciplinary in nature, drawing from both Dimer, Relaxation, Capsid and Protein folding.
Her Magic angle spinning study integrates concerns from other disciplines, such as Spectral resolution, Solid-state nuclear magnetic resonance, Molecular physics, Heteronuclear molecule and Anisotropy.
Between 2009 and 2021, her most popular works were:
- Mature HIV-1 capsid structure by cryo-electron microscopy and all-atom molecular dynamics (567 citations)
- HIV/Simian Immunodeficiency Virus (SIV) Accessory Virulence Factor Vpx Loads the Host Cell Restriction Factor SAMHD1 onto the E3 Ubiquitin Ligase Complex CRL4DCAF1 (143 citations)
- Tetramerization of SAMHD1 Is Required for Biological Activity and Inhibition of HIV Infection (122 citations)
In her most recent research, the most cited papers focused on:
Angela M. Gronenborn mainly focuses on Protein structure, Biochemistry, Capsid, Nuclear magnetic resonance spectroscopy and Crystallography.
Her Protein structure study combines topics in areas such as Dimer, Stereochemistry and Binding site.
Her Capsid research incorporates elements of Biophysics, Retrovirus, Trimer, Function and Magic angle spinning.
Her Nuclear magnetic resonance spectroscopy research is within the category of Nuclear magnetic resonance.
Her Crystallography study incorporates themes from Amino acid and Conformational isomerism.
Her biological study spans a wide range of topics, including Two-dimensional nuclear magnetic resonance spectroscopy and Ligand.
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