{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2025,10,27]],"date-time":"2025-10-27T04:46:17Z","timestamp":1761540377916},"reference-count":31,"publisher":"Wiley","issue":"11","license":[{"start":{"date-parts":[[2008,12,31]],"date-time":"2008-12-31T00:00:00Z","timestamp":1230681600000},"content-version":"vor","delay-in-days":2617,"URL":"http:\/\/onlinelibrary.wiley.com\/termsAndConditions#vor"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Protein Science"],"published-print":{"date-parts":[[2001,11]]},"abstract":"<jats:title>Abstract<\/jats:title><jats:p>Mass spectrometry has been used to examine the subunit interactions in the capsular F1 antigen from <jats:italic>Yersinia pestis<\/jats:italic>, the causative agent of the plague. Introducing the sample using nanoflow electrospray from solution conditions in which the protein remains in its native state and applying collisional cooling to minimize the internal energy of the ions, multiple subunit interactions have been maintained. This methodology revealed assemblies of the F1 antigen that correspond in mass to both 7\u2010mers and 14\u2010mers, consistent with interaction of two seven\u2010membered units. The difference between the calculated masses and those measured experimentally for these higher\u2010order oligomers was found to increase proportionately with the size of the complex. This is consistent with a solvent\u2010filled central cavity maintained on association of the 7\u2010mer to the 14\u2010mer. The charge states of the ions show that an average of one and four surface accessible basic side\u2010chains are involved in maintaining the interactions between the 7\u2010mer units and neighboring subunits, respectively. Taken together, these findings provide new information about the stoichiometry and packing of the subunits involved in the assembly of the capsular antigen structure. More generally, the data show that the symmetry and packing of macromolecular complexes can be determined solely from mass spectrometry, without any prior knowledge of higher order structure<\/jats:p>","DOI":"10.1110\/ps.11101","type":"journal-article","created":{"date-parts":[[2002,7,27]],"date-time":"2002-07-27T00:00:52Z","timestamp":1027728052000},"page":"2408-2413","source":"Crossref","is-referenced-by-count":21,"title":["Macromolecular organization of the <i>Yersinia pestis<\/i> capsular F1 antigen: Insights from time\u2010of\u2010flight mass spectrometry"],"prefix":"10.1002","volume":"10","author":[{"given":"Mark A.","family":"Tito","sequence":"first","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Julie","family":"Miller","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Kate F.","family":"Griffin","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"E. Diane","family":"Williamson","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Richard W.","family":"Titball","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Carol V.","family":"Robinson","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"311","published-online":{"date-parts":[[2008,12,31]]},"reference":[{"key":"e_1_2_6_2_1","doi-asserted-by":"crossref","first-page":"330","DOI":"10.1128\/jb.157.1.330-333.1984","article-title":"Nucleotide sequence of the papA gene encoding the Pap pilus subunit of human uropathogenic Escherichia coli","volume":"157","author":"Baga M.","year":"1984","journal-title":"J. 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