Supercharging by m-NBA Improves ETD-Based Quantification of Hydroxyl Radical Protein Footprinting.

ABSTRACT: Hydroxyl radical protein footprinting (HRPF) is an MS-based technique for analyzing protein structure based on measuring the oxidation of amino acid side chains by hydroxyl radicals diffusing in solution. Spatial resolution of HRPF is limited by the smallest portion of the protein for which oxidation amounts can be accurately quantitated. Previous work has shown electron transfer dissociation (ETD) to be the most reliable method for quantifying the amount of oxidation of each amino acid side chain in a mixture of peptide oxidation isomers, but efficient ETD requires high peptide charge states, which limits its applicability for HRPF. Supercharging reagents have been used to enhance peptide charge state for ETD analysis, but previous work has shown supercharging reagents to enhance charge s

SUBMITTER: Li X 

PROVIDER: S-EPMC4598181 | biostudies-literature | 2015 Aug

REPOSITORIES: biostudies-literature