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

		Cytochrome c^d			Apomyoglobin^f
z^b	Ubiquitin^c	protonated	deprotonated	Lysozyme^e	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	2532
		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

^aProteins 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).

^bIon charge state (absolute value).

^cValentine, S.J.; Counterman, A.E.; Clemmer, D.E. J. Am. Soc. Mass Spectrom. 1997, 8, 954.

^dShelimov, K. B.; Clemmer, D. E.; Hudgins, R. R.; Jarrold, M. F. J. Am. Chem. Soc. 1997, 119, 2240.

^eValentine, S.J.; Anderson, S.J.; Ellington, A.E; Clemmer, D.E. J. Phys. Chem. B 1997, 101, 3891.

^fLiu, Y.; Valentine, S. J.; Clemmer, D. E. (unpublished results).