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Originally published In Press as doi:10.1074/mcp.M100009-MCP200 on November 28, 2001.
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Molecular & Cellular Proteomics 1:132-138, 2002.
© 2002 by The American Society for Biochemistry and Molecular Biology, Inc.

Research

Hydrogen Exchange-Mass Spectrometry

Optimization of Digestion Conditions*

Lintao Wang, Hai Pan and David L. Smith{ddagger}

From the Department of Chemistry, University of Nebraska, Lincoln, Nebraska 68588-0304

The direct linkage between folded structures of proteins and their function has increased the need for high resolution structures. In addition, there is a need for analytical methods for detecting and locating changes in the folded structures of proteins under a wide variety of conditions. The rates at which hydrogens located at peptide amide linkages undergo isotopic exchange has become the basis for an important method for detecting such structural changes. When detected by mass spectrometry, hydrogen exchange can be used to study dilute solutions of large proteins and protein complexes with very high sensitivity. To locate structural changes, labeled proteins are often digested with acid proteases to form peptides whose hydrogen/deuterium levels are determined by mass spectrometry. This approach is successful only when the protein can be digested rapidly under conditions where isotope exchange is slow. This study describes how columns packed with immobilized pepsin can be used to reduce the digestion time and to provide an effective means for separating the pepsin from the isotopically labeled fragments. These columns are part of an on-line system that facilitates both rapid digestion of low concentrations of protein and concentration of the peptides.

{ddagger} To whom correspondence should be addressed. Tel.: 402-472-2794; Fax: 402-472-9402; E-mail: dsmith7{at}unl.edu.


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Copyright © 2002 by the American Society for Biochemistry and Molecular Biology.