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Annu Rev Biophys Biomol Struct. 2003;32:1-25. Epub 2003 Feb 18.

Protein analysis by hydrogen exchange mass spectrometry.

Author information

1
Department of Chemistry and Biochemistry University of Colorado, Boulder, Colorado 80309, USA. Andrew.Hoofnagle@uchsc.edu

Erratum in

  • Annu Rev Biophys Biomol Struct. 2005;34:vi.

Abstract

Mass spectrometry has provided a powerful method for monitoring hydrogen exchange of protein backbone amides with deuterium from solvent. In comparison to popular NMR approaches, mass spectrometry has the advantages of higher sensitivity, wider coverage of sequence, and the ability to analyze larger proteins. Proteolytic fragmentation of proteins following the exchange reaction provides moderate structural resolution, in some cases enabling measurements from single amides. The technique has provided new insight into protein-protein and protein-ligand interfaces, as well as conformational changes during protein folding or denaturation. In addition, recent studies illustrate the utility of hydrogen exchange mass spectrometry toward detecting protein motions relevant to allostery, covalent modifications, and enzyme function.

[Indexed for MEDLINE]

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