What is she best known for?
The fields of study she is best known for:
Dissociation, Analytical chemistry, Mass spectrometry, Stereochemistry and Tandem mass spectrometry are her primary areas of study.
Her work carried out in the field of Dissociation brings together such families of science as Ion, Protonation, Protein subunit, Protein quaternary structure and Peptide.
Her Analytical chemistry research is multidisciplinary, incorporating elements of Crystallography and Monolayer.
Her study focuses on the intersection of Mass spectrometry and fields such as Matrix-assisted laser desorption/ionization with connections in the field of Chromatography, Yeast, Bacteria, Electrospray and Positive blood culture.
Her research in Stereochemistry intersects with topics in Peptide bond, Macromolecule, Protein secondary structure and Residue.
The study incorporates disciplines such as Mass spectrum and Fragmentation in addition to Tandem mass spectrometry.
Her most cited work include:
- Mobile and localized protons: a framework for understanding peptide dissociation (753 citations)
- Influence of Peptide Composition, Gas-Phase Basicity, and Chemical Modification on Fragmentation Efficiency: Evidence for the Mobile Proton Model (659 citations)
- Interface Dipoles Arising from Self-Assembled Monolayers on Gold: UV−Photoemission Studies of Alkanethiols and Partially Fluorinated Alkanethiols (322 citations)
What are the main themes of her work throughout her whole career to date?
Vicki H. Wysocki focuses on Mass spectrometry, Dissociation, Ion, Analytical chemistry and Stereochemistry.
Her Mass spectrometry study combines topics from a wide range of disciplines, such as Structural biology and Ionization.
Vicki H. Wysocki interconnects Tandem mass spectrometry, Crystallography, Protonation, Protein subunit and Fragmentation in the investigation of issues within Dissociation.
Her Ion study incorporates themes from Molecule, Photochemistry and Monolayer.
Her studies in Analytical chemistry integrate themes in fields like Quadrupole and Tetramer.
She has researched Stereochemistry in several fields, including Oxazolone and Amino acid, Peptide bond, Peptide, Histidine.
She most often published in these fields:
- Mass spectrometry (34.51%)
- Dissociation (33.10%)
- Ion (24.65%)
What were the highlights of her more recent work (between 2017-2021)?
- Mass spectrometry (34.51%)
- Dissociation (33.10%)
- Ion (24.65%)
In recent papers she was focusing on the following fields of study:
Her scientific interests lie mostly in Mass spectrometry, Dissociation, Ion, Biophysics and Structural biology.
Her Mass spectrometry research is multidisciplinary, relying on both Computational chemistry, Docking, Macromolecule and Protein subunit, Protein quaternary structure.
Her Computational chemistry study frequently draws parallels with other fields, such as Tandem mass spectrometry.
Her biological study spans a wide range of topics, including Crystallography, Fragmentation, Ionization and Molecule.
Her study looks at the intersection of Molecule and topics like Ion trap with Fourier transform ion cyclotron resonance and Protonation.
Her work deals with themes such as Optoelectronics and Orbitrap, which intersect with Ion.
Between 2017 and 2021, her most popular works were:
- How many human proteoforms are there (219 citations)
- Programmable design of orthogonal protein heterodimers (58 citations)
- De novo design of protein logic gates (43 citations)
In her most recent research, the most cited papers focused on:
The scientist’s investigation covers issues in Mass spectrometry, Dissociation, Structural biology, Protein subunit and Protein structure.
Her Mass spectrometry study integrates concerns from other disciplines, such as Ion, Cofactor, Computational chemistry and Protein quaternary structure.
Her Computational chemistry research incorporates elements of Tandem mass spectrometry, Native protein and Reaction step.
Her Protein quaternary structure study frequently involves adjacent topics like Fragmentation.
The various areas that she examines in her Dissociation study include Ion trap, Molecule, Electrode and Analytical chemistry.
In her work, Biophysics is strongly intertwined with Histidine, which is a subfield of Protein structure.
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