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. Author manuscript; available in PMC: 2012 Jun 3.
Published in final edited form as: Proteins. 2007 Nov 1;69(2):270–284. doi: 10.1002/prot.21471

Table II.

Cross-links of HIV-1 Vif. Cross-linked residues identified by MALDI-TOF-MS and heavy water labeling of trypsin-digested monomeric, dimeric or trimeric forms of HIV-1 Vif. The cross-linking agent EDC specifically links lysine (K) to either aspartic acid (D) or glutamic acid (E). If more than one lysine or acid is within an identified fragment, all are listed. Linking residues are listed sequentially. Cross-linked residues in bold appear in Figure 4. Italics indicate that experimental molecular weights were consistent with theoretical molecular weights of both cross-links.

Monomer Dimer Trimer
K26, K34 E171, D172
Termini E45 Termini E45 Termini E45
Termini D61, E76 Termini D61, E76 Termini D61, E76
E2 K26, K34 E2 K26, K34 E2 K26, K34
E54, D61 K176, K179 E54, D61 K176, K179 E54, D61 K176, K179
E2 K141 E2 K141 E2 K141
E2 K176, K179, K181 E2 K176, K179,
K181
E2 K176, K179, K181
D14 K26, K34 D14 K26, K34 D14 K26, K34
K22, K26 E45 K22, K26 E45 K22, K26 E45
K26, K34 D78, E88 K26, K34 D78, E88 K26, K34 D78, E88
E45 K91, K92 E45 K91, K92 E45 K91, K92
E45 K92 E45 K92 E45 K92
D78, E88 K91, K92 D78, E88 K91, K92 D78, E88 K91, K92
E171, D172 K181 E171, D172 K181 E171, D172 K181
K34 E134 K34 E134
E45 K176, K179 E45 K176, K179
D61 K160, K168 D61 K160, K168
K92 E171, D172 K92 E171, D172
D14 K158, K160, K168
K34 Termini
K158, K160, K168 E171, D172
K158, K160, K168 Termini
K160, K168,
E171, D172
Termini
K160, K168,
E171, D172, K176,
K179
Termini
E171, D172 K181