| pubmed-article:16501223 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:16501223 | lifeskim:mentions | umls-concept:C0872079 | lld:lifeskim |
| pubmed-article:16501223 | lifeskim:mentions | umls-concept:C0597486 | lld:lifeskim |
| pubmed-article:16501223 | lifeskim:mentions | umls-concept:C0936012 | lld:lifeskim |
| pubmed-article:16501223 | lifeskim:mentions | umls-concept:C0449445 | lld:lifeskim |
| pubmed-article:16501223 | pubmed:issue | 3 | lld:pubmed |
| pubmed-article:16501223 | pubmed:dateCreated | 2006-2-27 | lld:pubmed |
| pubmed-article:16501223 | pubmed:abstractText | We have developed a new approach for the analysis of interacting interfaces in protein complexes and protein quaternary structure based on cross-linking in the solid state. Protein complexes are freeze-dried under vacuum, and cross-links are introduced in the solid phase by dehydrating the protein in a nonaqueous solvent creating peptide bonds between amino and carboxyl groups of the interacting peptides. Cross-linked proteins are digested into peptides with trypsin in both H2(16)O and H(2)18O and then readily distinguished in mass spectra by characteristic 8 atomic mass unit (amu) shifts reflecting incorporation of two 18O atoms into each C terminus of proteolytic peptides. Computer analysis of mass spectrometry (MS) and MS/MS data is used to identify the cross-linked peptides. We demonstrated specificity and reproducibility of our method by cross-linking homo-oligomeric protein complexes of glutathione-S-transferase (GST) from Schistosoma japonicum alone or in a mixture of many other proteins. Identified cross-links were predominantly of amide origin, but six esters and thioesters were also found. The cross-linked peptides were validated against the GST monomer and dimer X-ray structures and by experimental (MS/MS) analyses. Some of the identified cross-links matched interacting peptides in the native 3D structure of GST, indicating that the structure of GST and its oligomeric complex remained primarily intact after freeze-drying. The pattern of oligomeric GST obtained in solid state was the same as that obtained in solution by Ru (II) Bpy(3)2+ catalyzed, oxidative "zero-length" cross-linking, confirming that it is feasible to use our strategy for analyzing the molecular interfaces of interacting proteins or peptides. | lld:pubmed |
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| pubmed-article:16501223 | pubmed:language | eng | lld:pubmed |
| pubmed-article:16501223 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:16501223 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:16501223 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:16501223 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:16501223 | pubmed:month | Mar | lld:pubmed |
| pubmed-article:16501223 | pubmed:issn | 0961-8368 | lld:pubmed |
| pubmed-article:16501223 | pubmed:author | pubmed-author:El-ShafeyAhme... | lld:pubmed |
| pubmed-article:16501223 | pubmed:author | pubmed-author:SmithRichard... | lld:pubmed |
| pubmed-article:16501223 | pubmed:author | pubmed-author:YoungMalin... | lld:pubmed |
| pubmed-article:16501223 | pubmed:author | pubmed-author:KeryVladimirV | lld:pubmed |
| pubmed-article:16501223 | pubmed:author | pubmed-author:TolicNikolaN | lld:pubmed |
| pubmed-article:16501223 | pubmed:author | pubmed-author:SaleKennethK | lld:pubmed |
| pubmed-article:16501223 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:16501223 | pubmed:volume | 15 | lld:pubmed |
| pubmed-article:16501223 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:16501223 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:16501223 | pubmed:pagination | 429-40 | lld:pubmed |
| pubmed-article:16501223 | pubmed:dateRevised | 2009-11-18 | lld:pubmed |
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| pubmed-article:16501223 | pubmed:meshHeading | pubmed-meshheading:16501223... | lld:pubmed |
| pubmed-article:16501223 | pubmed:year | 2006 | lld:pubmed |
| pubmed-article:16501223 | pubmed:articleTitle | "Zero-length" cross-linking in solid state as an approach for analysis of protein-protein interactions. | lld:pubmed |
| pubmed-article:16501223 | pubmed:affiliation | Cell Biology and Biochemistry, Pacific Northwest National Laboratory, 902 Battelle Blvd., P.O. Box 999, K4-12, Richland, WA 99354, USA. | lld:pubmed |
| pubmed-article:16501223 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:16501223 | pubmed:publicationType | Evaluation Studies | lld:pubmed |
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