期刊
BIOCHIMICA ET BIOPHYSICA ACTA-PROTEINS AND PROTEOMICS
卷 1834, 期 6, 页码 1230-1238出版社
ELSEVIER SCIENCE BV
DOI: 10.1016/j.bbapap.2013.02.023
关键词
Protein folding and unfolding; Fast photochemical oxidation of proteins (FPOP); Protein footprinting; Barstar Mass spectrometry; Data processing
资金
- National Institute of General Medical Sciences of the NIH [8 P41 GM103422-35]
Mass spectrometry-based protein footprinting reveals regional and even amino-acid structural changes and fills the gap for many proteins and protein interactions that cannot be studied by X-ray crystallography or NMR spectroscopy. Hydroxyl radical-mediated labeling has proven to be particularly informative in this pursuit because many solvent-accessible residues can be labeled by center dot OH in a protein or protein complex, thus providing more coverage than does specific amino-acid modifications. Finding all the center dot OH-labeling sites requires LC/MS/MS analysis of a proteolyzed sample, but data processing is daunting without the help of automated software. We describe here a systematic means for achieving a comprehensive residue-resolved analysis of footprinting data in an efficient manner, utilizing software common to proteomics core laboratories. To demonstrate the method and the utility of center dot OH-mediated labeling, we show that FPOP easily distinguishes the buried and exposed residues of barstar in its folded and unfolded states. This article is part of a Special Issue entitled: Mass spectrometry in structural biology. (C) 2013 Elsevier B.V. All rights reserved.
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