Richard W. Vachet

Using mass spectrometry to study copper-protein binding under native and non-native conditions: beta-2-microglobulin.

Transition metal-peptide binding studied by metal-catalyzed oxidation reactions and mass spectrometry.

The effect of histidine oxidation on the dissociation patterns of peptide ions.

Cu(II) organizes beta-2-microglobulin oligomers but is released upon amyloid formation.

Protein surface mapping using diethylpyrocarbonate with mass spectrometric detection.

Probing protein structure by amino acid-specific covalent labeling and mass spectrometry.

Matrix-assisted laser desorption ionization-mass spectrometry signal enhancement of peptides after selective extraction with polymeric reverse micelles.

Electron transfer dissociation of modified peptides and proteins.

Coordination sphere tuning of the electron transfer dissociation behavior of Cu(II)-peptide complexes.

Characterization of surface ligands on functionalized magnetic nanoparticles using laser desorption/ionization mass spectrometry (LDI-MS).

Identifying Zn-bound histidine residues in metalloproteins using hydrogen-deuterium exchange mass spectrometry.

Exploring salt bridge structures of gas-phase protein ions using multiple stages of electron transfer and collision induced dissociation.

Mass spectrometric detection of nanoparticle host-guest interactions in cells.

Molecular histology: More than a picture.

Inkjet-printed gold nanoparticle surfaces for the detection of low molecular weight biomolecules by laser desorption/ionization mass spectrometry.

Quantitative imaging of 2 nm monolayer-protected gold nanoparticle distributions in tissues using laser ablation inductively-coupled plasma mass spectrometry (LA-ICP-MS).

Quantitative Differentiation of Cell Surface-Bound and Internalized Cationic Gold Nanoparticles Using Mass Spectrometry.

Polymer-mediated ternary supramolecular interactions for sensitive detection of peptides.

Gradient and Patterned Protein Films Stabilized via Nanoimprint Lithography for Engineered Interactions with Cells.

Increased β-Sheet Dynamics and D-E Loop Repositioning Are Necessary for Cu(II)-Induced Amyloid Formation by β-2-Microglobulin.

Small molecule-mediated inhibition of β-2-microglobulin-based amyloid fibril formation.

Disruption of the open conductance in the β-tongue mutants of Cytolysin A.

Covalent labeling-mass spectrometry with non-specific reagents for studying protein structure and interactions.

Covalent labeling and mass spectrometry reveal subtle higher order structural changes for antibody therapeutics.

Covalent Labeling with Diethylpyrocarbonate: Sensitive to the Residue Microenvironment, Providing Improved Analysis of Protein Higher Order Structure by Mass Spectrometry.

Efficient enrichment of glycopeptides by supramolecular nanoassemblies that use proximity-assisted covalent binding.

Structural Heterogeneity in the Preamyloid Oligomers of β-2-Microglobulin.

Polymeric nanoassemblies for enrichment and detection of peptides and proteins in human breast milk.

Higher-Order Structure Influences the Kinetics of Diethylpyrocarbonate Covalent Labeling of Proteins.

Epigallocatechin-3-gallate Inhibits Cu(II)-Induced β-2-Microglobulin Amyloid Formation by Binding to the Edge of Its β-Sheets.

Measuring the Energy Barrier of the Structural Change That Initiates Amyloid Formation.

Reconstruction, analysis, and segmentation of LA-ICP-MS imaging data using Python for the identification of sub-organ regions in tissues.

Covalent Labeling/Mass Spectrometry of Monoclonal Antibodies with Diethylpyrocarbonate: Reaction Kinetics for Ensuring Protein Structural Integrity.

Protein-Ligand Affinity Determinations Using Covalent Labeling-Mass Spectrometry.

MEMBRANE PROTEIN STRUCTURES AND INTERACTIONS FROM COVALENT LABELING COUPLED WITH MASS SPECTROMETRY.

Enhanced and Selective MALDI-MS Detection of Peptides via the Nanomaterial-Dependent Coffee Ring Effect.

In Vivo Editing of Macrophages through Systemic Delivery of CRISPR-Cas9-Ribonucleoprotein-Nanoparticle Nanoassemblies.

A programmable chemical switch based on triggerable Michael acceptors.