Work

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

Year: 2008

Type: review

Abstract: For many years, amino acid-specific covalent labeling has been a valuable tool to study protein structure and protein interactions, especially for systems that are difficult to study by other means. These covalent labeling methods typically map protein structure and interactions by measuring the differential reactivity of amino acid side chains. The reactivity of amino acids in proteins generally depends on the accessibility of the side chain to the reagent, the inherent reactivity of the label and the reactivity of the amino acid side chain. Peptide mass mapping with ESI- or MALDI-MS and peptide sequencing with tandem MS are typically employed to identify modification sites to provide site-specific structural information. In this review, we describe the reagents that are most commonly used in these residue-specific modification reactions, details about the proper use of these covalent labeling reagents, and information about the specific biochemical problems that have been addressed with covalent labeling strategies.

Source: Mass Spectrometry Reviews

DOI: 10.1002/mas.20203

Authors: Vanessa Leah Mendoza, Richard W. Vachet

Institution: University of Massachusetts Amherst

Language: English

Topic: Mass Spectrometry Techniques and Applications

Subfield: Spectroscopy

Field: Chemistry

Domain: Physical Sciences

Open Access status: green

Funders: National Institutes of Health, National Institute of General Medical Sciences

Awards: Copper-Induced Amyloidosis Studied by Mass Spectrometry, Chemistry Biology Interface Predoctoral Training Grant