Deciphering structure and topology of conserved COG2042 orphan proteins-3

Abstract

<p><b>Copyright information:</b></p><p>Taken from "Deciphering structure and topology of conserved COG2042 orphan proteins"</p><p>BMC Structural Biology 2005;5():3-3.</p><p>Published online 8 Feb 2005</p><p>PMCID:PMC549553.</p><p>Copyright © 2005 Armengaud et al; licensee BioMed Central Ltd.</p>ith a trypsin/SSO0551 protein ratio of 1/20 (w/w). The products were then resolved onto a C8 reverse phase chromatographic column and the different UV absorbing fractions were analyzed by MALDI-TOF. The spectrum obtained with the fraction eluting at 40–50 % acetonitrile is shown. The asterisk labels a peak arising from trypsin autolysis. Peaks that could be assigned are identified with numbers (experimental , residues, Δmass in ppm compared to theoretical [M+H]average mass): (19198.4, [1–166], -1), (15478.7, [32–166], -53), (15191.2, [35–166], +153), (12883.4, [52–162] or [56–166], -46 or -43), (12724.2, [57–166], +193), (10603.8, [76–166], +51), (10220.1, [79–166], +77), (9257.2, [83–162], +63) and (7717.0, [101–166], -134). Peptides and , complementary of and , were not observed in this spectrum but in another fraction from the C8 reverse-phase chromatography corresponding to smaller peptides