Collision cross sections (in Å2) of individual protein charge states.a



z b Ubiquitin c Cytochrome c d Lysozyme e Apomyoglobin f
protonated deprotonated protonated deprotonated
3 1139
4 1004 1153 1174 1459
1059
5 1027 1196 1246 1313 1484 1433
1137 1340
1239
6 1041 1393 1351 1355 1562 1539
1220 1244 1535 1959 1795
1525 1602 1244
7 1317 1785 1267 1364 2250 1743
1580 1247 1586 1674 2025
2007 2057 1581
1620
8 1442 1845 1334 1363 1673 2203
1622 1250 1760 1781 2352 1624
2061 2203
1702
9 1649 2215 1707 1407 1758 2535
1964 2024 1899 2659 1717
2384 2704
10 1732 2226 2207 1446 1897 2656
1961 2796
2390
11 1802 2303 2305 2459 2942 2879
12 2335 2340 2525 3044 2968
13 2391 2598 3136 3057
14 2473 2672 3143 3136
15 2579 2733 3230 3226
16 2679 2823 3313 3281
17 2723 2894 3384 3395
18 2766 2989 3489
19 2800 3570
20 2889 3682
21 3792
22 3815


a Proteins are listed from left to right in order of molecular weight. Unless otherwise denoted, cross sections are provided for protonated ions. Multiple values corresponding to a single protein charge state indicate the observation of multiple resolvable peak maxima. Protein sources are as follows: ubiquitin (bovine); cytochrome c (horse), lysozyme (turkey egg white), and apomyoglobin (sperm whale).
b Ion charge state (absolute value).
c Valentine, S.J.; Counterman, A.E.; Clemmer, D.E. J. Am. Soc. Mass Spectrom. 1997, 8, 954.
d Shelimov, K. B.; Clemmer, D. E.; Hudgins, R. R.; Jarrold, M. F. J. Am. Chem. Soc. 1997, 119, 2240.
e Valentine, S.J.; Anderson, S.J.; Ellington, A.E; Clemmer, D.E. J. Phys. Chem. B 1997, 101, 3891.
f Liu, Y.; Valentine, S. J.; Clemmer, D. E. (unpublished results).