Mass spectrometry-based protein footprinting for higher-order structure analysis: fundamentals and applications

XR Liu, MM Zhang, ML Gross - Chemical reviews, 2020‏ - ACS Publications
Proteins adopt different higher-order structures (HOS) to enable their unique biological
functions. Understanding the complexities of protein higher-order structures and dynamics …

Arsenic binding to proteins

S Shen, XF Li, WR Cullen, M Weinfeld, XC Le - Chemical reviews, 2013‏ - ACS Publications
Arsenic is a trace element found in the earth, s crust at an average concentration of∼ 5 μg/g
(ppm). Although its relative abundance in the earth, s crust is about 54th, arsenic can …

Hydroxyl radical-mediated modification of proteins as probes for structural proteomics

G Xu, MR Chance - Chemical reviews, 2007‏ - ACS Publications
“Footprinting” refers to assays that examine ligand binding and conformational changes by
determining the solvent accessibility of the backbone, bases, or side chain structures of …

Chemical modifications in therapeutic protein aggregates generated under different stress conditions

Q Luo, MK Joubert, R Stevenson, RR Ketchem… - Journal of Biological …, 2011‏ - ASBMB
In this study, we characterized the chemical modifications in the monoclonal antibody (IgG 2)
aggregates generated under various conditions, including mechanical, chemical, and …

Radiolytic protein footprinting with mass spectrometry to probe the structure of macromolecular complexes

K Takamoto, MR Chance - Annu. Rev. Biophys. Biomol. Struct., 2006‏ - annualreviews.org
Structural proteomics approaches using mass spectrometry are increasingly used in biology
to examine the composition and structure of macromolecules. Hydroxyl radical–mediated …

The Amyloid-β Peptide of Alzheimer's Disease Binds CuI in a Linear Bis-His Coordination Environment: Insight into a Possible Neuroprotective Mechanism for the …

J Shearer, VA Szalai - Journal of the American Chemical Society, 2008‏ - ACS Publications
Oxidative stress has been suggested to contribute to neuronal apoptosis associated with
Alzheimer's disease (AD). Copper may participate in oxidative stress through redox-cycling …

Protein structure and dynamics studied by mass spectrometry: H/D exchange, hydroxyl radical labeling, and related approaches

L Konermann, X Tong, Y Pan - Journal of Mass Spectrometry, 2008‏ - Wiley Online Library
Mass spectrometry (MS) plays a central role in studies on protein structure and dynamics.
This review highlights some of the recent developments in this area, with focus on …

Using mass spectrometry‐based methods to understand amyloid formation and inhibition of alpha‐synuclein and amyloid beta

WJ Wagner, ML Gross - Mass spectrometry reviews, 2024‏ - Wiley Online Library
Amyloid fibrils, insoluble β‐sheets structures that arise from protein misfolding, are
associated with several neurodegenerative disorders. Many small molecules have been …

A comparison of methionine, histidine and cysteine in copper(i)-binding peptides reveals differences relevant to copper uptake by organisms in diverse environments

JT Rubino, MP Chenkin, M Keller… - Metallomics, 2011‏ - academic.oup.com
The N-terminal, extracellular regions of eukaryotic high affinity copper transport (Ctr)
proteins vary in composition of the Cu (i) binding amino acids: methionine, histidine, and …

Structural proteomics of macromolecular assemblies using oxidative footprinting and mass spectrometry

JQ Guan, MR Chance - Trends in biochemical sciences, 2005‏ - cell.com
Understanding the composition, structure and dynamics of macromolecules and their
assemblies is at the forefront of biological science today. Hydroxyl-radical-mediated protein …