. Author manuscript; available in PMC: 2014 Dec 31.

Published in final edited form as: Biochemistry. 2013 Dec 17;52(52):9470–9481. doi: 10.1021/bi401080k

Table 1.

Intrapeptide Peptides

Theoretical MH⁺	d₀-m/z	d₄-m/Z	positive charge	Sequenced d₀- m/z	Exp MH⁺	Δ m/z	Intensity	Lys1	Lys2

2303.2070	768.41	769.74	3	768.41	2303.1965	0.0105	139	94	96
2303.2069	768.41	769.74	3	768.43	2303.1946	0.0123	1030	133	140
2347.2509	783.09	784.42	3	783.06	2347.2312	0.0197	230	206	208
1672.8467	836.93^*		2	836.93	1672.7819	0.0648	59	88	94
1717.9165	859.46	861.46	2	859.45	1717.9421	−0.0256	87	96	106
2616.4037	872.81	874.14	3	872.79	2616.3601	0.0436	157	45	59
3728.8699	932.97	933.97	4	932.97	3728.8325	ro.0374	70	40	45
2016.1017	1008.55	1010.55	2	1008.52	2016.0919	0.0098	1360	12	23
2109.1120	1055.06	1057.06	2	1055.06	2109.1335	−0.0215	162	238	239

Table 1 is a compilation of the intrapeptide cross-linked peptides. These peptides were found in both 0.2 mg/mL and 1.0 mg/mL apoA-l. The theoretical and experimental m/z for the intact cross-linked peptide are given, along with m/z for the charge state sequenced and its theoretical m/z. Δ m/z is the difference between the theoretical and experimental m/z for the protonated, intact cross-linked peptide. Maximum ion intensity and amino acid position are listed in the last three rows.

Sequenced from experiments that used only d₀-BS³.