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. 2010 Feb 10;11(Suppl 1):S13. doi: 10.1186/1471-2164-11-S1-S13

Table 1.

Influence of background removal on the recovery of BSA, ADH and TRF in MS/MS spectra of 100 fmol test samples. The original number of MS/MS spectra for the BSA (bovine serum albumine), ADH (yeast alcoholdehydrogenase) and TRF (human transferring) datasets (recorded on a DecaXP machine) are 2679, 2325 and 2608 respectively. The intensity threshold s (column 3) describes the search of the sequence ladder (length n in column 2) within the 15%, 20%, 25% or 30% top peaks (100% - all peaks are considered). The following three columns show the MS Cleaner output - number of spectra with background removal, number of unselected spectra and the MS Cleaner CPU time on a single-processor Windows XP computer (Pentium IV 2.4 GHz; to get exact measurements of computation time, we did not use the cluster version). The remaining four columns present the MASCOT output - the CPU time on the same machine, the protein score, the number of spectra matching peptides in a MASCOT search and the final sequence coverage. For each dataset, the first line shows the results for the case when MS Cleaner is not used for pre-processing and the MS/MS data is immediately interpreted by MASCOT.

protein sequence ladder length n intensity threshold s [%] cleaned spectra bad spectra MS Cleaner time [min] MASCOT time [min] MASCOT score queries matched sequence coverage
BSA 0 100 - - - 61 586 89 55

3 100 1664 1015 3.92 44 720 91 57
3 15 390 2289 1.21 17 1991 84 52
3 20 490 2189 1.40 21 2108 87 57
3 25 601 2078 1.61 26 2114 89 57
3 30 688 1991 1.75 29 2114 90 57

4 100 940 1739 3.80 36 2108 91 57
4 15 260 2419 0.91 12 1875 78 47
4 20 321 2358 1.06 14 1911 80 47
4 25 380 2299 1.25 18 2114 86 57
4 30 441 2238 1.30 19 2114 89 57

5 100 593 2086 3.82 26 2108 91 57
5 15 174 2505 0.60 9 1579 60 41
5 20 232 2447 0.85 11 1809 72 44
5 25 281 2398 1.00 13 1963 81 49
5 30 313 2366 0.85 14 2058 86 54

ADH 0 100 - - - 64 242 39 39

3 100 1446 879 4.15 45 327 34 39
3 15 269 2056 0.88 12 673 29 35
3 20 347 1978 1.10 13 696 31 37
3 25 440 1885 1.33 17 697 32 37
3 30 697 1628 1.53 20 697 33 37

4 100 902 1423 4.15 35 733 34 39
4 15 173 2152 0.58 7 562 26 28
4 20 216 2109 0.71 9 673 30 35
4 25 271 2054 0.90 12 607 28 33
4 30 325 2000 1.05 13 697 32 37

5 100 594 1731 4.20 23 712 33 39
5 15 94 2231 0.35 5 311 15 21
5 20 125 2200 0.46 6 366 17 25
5 25 145 2180 0.53 7 434 19 26
5 30 186 2139 0.66 9 589 24 31

TRF 0 100 - - - 52 588 86 47

3 100 1587 1021 3.57 42 768 87 49
3 15 373 2235 1.00 17 1988 86 49
3 20 485 2123 1.23 20 1988 86 49
3 25 568 2040 1.36 24 1998 87 49
3 30 639 1969 0.78 27 1998 87 49

4 100 864 1744 3.62 34 1973 87 49
4 15 231 2377 0.70 11 1987 81 49
4 20 298 2310 0.86 13 1988 84 49
4 25 360 2248 1.00 16 1988 85 49
4 30 414 2194 1.12 19 1998 87 49

5 100 540 2068 3.63 23 1973 87 49
5 15 164 2444 0.55 9 1785 68 45
5 20 194 2414 0.61 10 1890 74 47
5 25 245 2363 0.75 12 1957 80 48
5 30 286 2322 0.86 14 1968 84 48