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| Content Provider | Royal Society of Chemistry (RSC) |
|---|---|
| Author | Lees-Miller, Susan P. Hepburn, Morgan Sheff, Joey G. Yu, Yaping Schriemer, David C. |
| Copyright Year | 2017 |
| Abstract | Hydrogen-deuterium exchange mass spectrometry (HX-MS) has made important contributions to the study of protein structure and function. Unfortunately, it is not known for low limits of detection, when compared with other forms of peptide-based or bottom-up protein MS methods. Systems perform poorly on sub-pmol quantities of protein states with greater than 300 kDa of unique sequences. The HX-MS analysis of complex protein states would be possible if proteomics-grade configurations could be used reliably, but temperature and temporal constraints have proven to be significant design challenges. Here, we describe an integrated HX-MS ion source operating on a vented-column geometry, which brings regulated column cooling right to the spray tip. The design offers chromatographic peak widths of 2–6 s (FWHM). It provides stable operation at 500 nL min−1, while retaining deuteration levels comparable to conventional geometries. We demonstrate at least a 50-fold improvement in protein consumption levels, and illustrate robustness by measuring peptide-averaged protection factors for 90% of DNA-PKcs, a 469 kDa protein, from 0.5 pmol injections. |
| Starting Page | 904 |
| Ending Page | 910 |
| Page Count | 7 |
| File Format | HTM / HTML PDF |
| ISSN | 00032654 |
| Volume Number | 142 |
| Issue Number | 6 |
| Journal | The Analyst |
| DOI | 10.1039/c6an02707e |
| Language | English |
| Publisher | Royal Society of Chemistry |
| Access Restriction | Open |
| Subject Keyword | DNA-PKcs Full width at half maximum Ion Mass spectrometry Protein structure Protein Chromatography Molecular geometry |
| Content Type | Text |
| Resource Type | Article |
| Subject | Spectroscopy Environmental Chemistry Analytical Chemistry Biochemistry Electrochemistry |
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