What is he best known for?
The fields of study he is best known for:
Rolf Boelens focuses on Stereochemistry, Nuclear magnetic resonance spectroscopy, Protein structure, Biochemistry and DNA.
His Stereochemistry research is multidisciplinary, incorporating perspectives in lac operon, DNA-binding protein and NMR spectra database.
His Nuclear magnetic resonance spectroscopy research includes elements of Proton NMR, Crystallography, Zinc finger, Rhodobacter sphaeroides and Thymine.
Rolf Boelens has included themes like Dimer, Molecule, Hydrogen bond and Molecular dynamics in his Crystallography study.
His DNA research focuses on DNA-binding domain and how it connects with HMG-box and Protein secondary structure.
His work in the fields of Docking, such as Searching the conformational space for docking, overlaps with other areas such as Haddock.
His most cited work include:
- HADDOCK: a protein-protein docking approach based on biochemical or biophysical information. (1999 citations)
- Dynamic Readers for 5-(Hydroxy)Methylcytosine and Its Oxidized Derivatives (718 citations)
- Solution structure of the glucocorticoid receptor DNA-binding domain (504 citations)
What are the main themes of his work throughout his whole career to date?
His main research concerns Nuclear magnetic resonance spectroscopy, Crystallography, Stereochemistry, Biochemistry and DNA.
His research in Nuclear magnetic resonance spectroscopy intersects with topics in Molecule, Two-dimensional nuclear magnetic resonance spectroscopy and Molecular dynamics.
His Crystallography study combines topics in areas such as Protein secondary structure, Dimer, Repressor, Hydrogen bond and Protein structure.
The concepts of his Stereochemistry study are interwoven with issues in Lac repressor and DNA-binding domain.
Many of his studies on Biochemistry apply to Biophysics as well.
His research integrates issues of Transcription, DNA-binding protein and Cell biology in his study of DNA.
He most often published in these fields:
- Nuclear magnetic resonance spectroscopy (25.06%)
- Crystallography (24.32%)
- Stereochemistry (23.57%)
What were the highlights of his more recent work (between 2011-2020)?
- Biochemistry (21.09%)
- Biophysics (9.68%)
- Nuclear magnetic resonance spectroscopy (25.06%)
In recent papers he was focusing on the following fields of study:
His primary areas of study are Biochemistry, Biophysics, Nuclear magnetic resonance spectroscopy, Crystallography and DNA.
The Biophysics study combines topics in areas such as Protein domain, Protein folding, Molecular biology, Protein–protein interaction and Binding site.
His Binding site study which covers Plasma protein binding that intersects with Protein structure.
His Nuclear magnetic resonance spectroscopy study is within the categories of Nuclear magnetic resonance and Stereochemistry.
His study in Crystallography is interdisciplinary in nature, drawing from both Dimer, Molecule and Molecular model.
The study incorporates disciplines such as RNA, RNA-binding protein and DNA-binding protein in addition to DNA.
Between 2011 and 2020, his most popular works were:
- Dynamic Readers for 5-(Hydroxy)Methylcytosine and Its Oxidized Derivatives (718 citations)
- New insights into the structure and composition of technical lignins: a comparative characterisation study (348 citations)
- Hsp90-Tau complex reveals molecular basis for specificity in chaperone action (188 citations)
In his most recent research, the most cited papers focused on:
Rolf Boelens spends much of his time researching Biochemistry, Biophysics, Cell biology, Nuclear magnetic resonance spectroscopy and DNA repair.
His studies deal with areas such as Protein structure, Genetics, Binding site and Protein domain as well as Biophysics.
His Protein structure research is multidisciplinary, relying on both Molecular dynamics, Gene isoform, Molecule, RNase P and Monomer.
His work deals with themes such as Transcription factor and Daf-16, which intersect with Cell biology.
Rolf Boelens interconnects Folding, Bacterial outer membrane, Bama, Protein dynamics and Transmembrane domain in the investigation of issues within Nuclear magnetic resonance spectroscopy.
His DNA repair study integrates concerns from other disciplines, such as DNA damage and DNA-binding protein.
This overview was generated by a machine learning system which analysed the scientist’s
body of work. If you have any feedback, you can
contact us
here.
