| pubmed-article:12512095 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:12512095 | lifeskim:mentions | umls-concept:C0220806 | lld:lifeskim |
| pubmed-article:12512095 | lifeskim:mentions | umls-concept:C0033684 | lld:lifeskim |
| pubmed-article:12512095 | lifeskim:mentions | umls-concept:C0037813 | lld:lifeskim |
| pubmed-article:12512095 | lifeskim:mentions | umls-concept:C0678594 | lld:lifeskim |
| pubmed-article:12512095 | lifeskim:mentions | umls-concept:C2603343 | lld:lifeskim |
| pubmed-article:12512095 | lifeskim:mentions | umls-concept:C0282183 | lld:lifeskim |
| pubmed-article:12512095 | lifeskim:mentions | umls-concept:C0449445 | lld:lifeskim |
| pubmed-article:12512095 | pubmed:issue | 2 | lld:pubmed |
| pubmed-article:12512095 | pubmed:dateCreated | 2003-1-3 | lld:pubmed |
| pubmed-article:12512095 | pubmed:abstractText | Mass spectrometric analysis of wild-type proteins that have been covalently modified by bifunctional cross-linking reagents and then digested proteolytically can be used to obtain low-resolution distance constraints, which can be useful for protein structure determination. Limitations of this approach include time-consuming separation steps, such as the separation of internally cross-linked protein monomers from covalent dimers, and a susceptibility to artifacts due to low levels of natural and man-made peptide modifications that can be mistaken for cross-linked species. The results presented here show that when a crude cross-linked protein mixture is injected into an electrospray ionization Fourier transform mass spectrometry (ESI-FTMS) instrument, the cross-link positions can be localized by fragmentation and mass spectrometry on the 'gas-phase purified' singly internally cross-linked monomer. Our results show that reaction of ubiquitin with the homobifunctional lysine-lysine cross-linking reagent dissuccinimidyl suberate (DSS) resulted in two cross-links consistent with the known ubiquitin tertiary structure (K6-K11 and K48-K63). Because no protein or peptide chemistry steps are needed, other than the initial cross-linking, this new top down approach appears well suited for high-throughput experiments with multiple cross-linkers and reaction conditions. Published in 2002 by John Wiley & Sons, Ltd. | lld:pubmed |
| pubmed-article:12512095 | pubmed:language | eng | lld:pubmed |
| pubmed-article:12512095 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12512095 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:12512095 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12512095 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12512095 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12512095 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:12512095 | pubmed:issn | 0951-4198 | lld:pubmed |
| pubmed-article:12512095 | pubmed:author | pubmed-author:YoungMalin... | lld:pubmed |
| pubmed-article:12512095 | pubmed:author | pubmed-author:KruppaGary... | lld:pubmed |
| pubmed-article:12512095 | pubmed:author | pubmed-author:SchoenigerJos... | lld:pubmed |
| pubmed-article:12512095 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:12512095 | pubmed:volume | 17 | lld:pubmed |
| pubmed-article:12512095 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:12512095 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:12512095 | pubmed:pagination | 155-62 | lld:pubmed |
| pubmed-article:12512095 | pubmed:dateRevised | 2006-11-15 | lld:pubmed |
| pubmed-article:12512095 | pubmed:meshHeading | pubmed-meshheading:12512095... | lld:pubmed |
| pubmed-article:12512095 | pubmed:meshHeading | pubmed-meshheading:12512095... | lld:pubmed |
| pubmed-article:12512095 | pubmed:meshHeading | pubmed-meshheading:12512095... | lld:pubmed |
| pubmed-article:12512095 | pubmed:meshHeading | pubmed-meshheading:12512095... | lld:pubmed |
| pubmed-article:12512095 | pubmed:meshHeading | pubmed-meshheading:12512095... | lld:pubmed |
| pubmed-article:12512095 | pubmed:meshHeading | pubmed-meshheading:12512095... | lld:pubmed |
| pubmed-article:12512095 | pubmed:meshHeading | pubmed-meshheading:12512095... | lld:pubmed |
| pubmed-article:12512095 | pubmed:meshHeading | pubmed-meshheading:12512095... | lld:pubmed |
| pubmed-article:12512095 | pubmed:meshHeading | pubmed-meshheading:12512095... | lld:pubmed |
| pubmed-article:12512095 | pubmed:year | 2003 | lld:pubmed |
| pubmed-article:12512095 | pubmed:articleTitle | A top down approach to protein structural studies using chemical cross-linking and Fourier transform mass spectrometry. | lld:pubmed |
| pubmed-article:12512095 | pubmed:affiliation | Sandia National Laboratories, Livermore, CA 94551-0969, USA. gkruppa@sandia.gov | lld:pubmed |
| pubmed-article:12512095 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:12512095 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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