Journal
MASS SPECTROMETRY REVIEWS
Volume 25, Issue 1, Pages 158-170Publisher
WILEY
DOI: 10.1002/mas.20064
Keywords
deuterium; electrospray; MALDI; protein folding; conformation
Categories
Funding
- NCI NIH HHS [R24-CA088339] Funding Source: Medline
- NCRR NIH HHS [P20-RR016480] Funding Source: Medline
- NIGMS NIH HHS [R01-GM070590, R01-GM068901] Funding Source: Medline
- NATIONAL CANCER INSTITUTE [R24CA088339] Funding Source: NIH RePORTER
- NATIONAL CENTER FOR RESEARCH RESOURCES [P20RR016480] Funding Source: NIH RePORTER
- NATIONAL INSTITUTE OF GENERAL MEDICAL SCIENCES [R01GM068901, R01GM070590] Funding Source: NIH RePORTER
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Hydrogen exchange coupled to mass spectrometry (MS) has become a valuable analytical tool for the stud), of protein dynamics. By combining information about protein dynamics with more classical functional data, a more thorough understanding of protein function can be obtained. In many cases, protein dynamics are directly related to specific protein functions such as conformational changes during enzyme activation or protein movements during binding. The method is made possible because labile backbone hydrogens in a protein will exchange with deuterium atoms when the protein is placed in a D2O solution. The subsequent increase in protein mass over time is measured with high-resolution MS. The location of the deuterium incorporation is determined by monitoring deuterium incorporation in peptic fragments that are produced after the labeling reaction. In this review, we will summarize the general principles of the method, discuss the latest variations on the experimental protocol that probe different types of protein movements, and review other recent work and improvements in the field. (C) 2005 Wiley Periodicals, Inc.
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