Table 1.
The difference in enthalpy formation of all 24 identified intra-molecular cross-link sites. The six energetically favourable sites, shown here in bold, were aligned to ECM binding sites of the human collagen type I sequence. Column 1 gives the site number, columns two to four highlight the cross-linked residue pair between two of the three polypeptide chains (labelled using the UniProt residue number and the triple helical residue number shown in brackets) and the fifth column lists the change in enthalpy (kcal/mol).
| Cross-link | Chain α1 (a) | Chain α1 (b) | Chain α2 | ΔEnthalpy |
|---|---|---|---|---|
| 1 | 229ARG(62) | 226LYS(59) | – | |
| 2 | 257ARG(90) | 183LYS(87) | − 13.572 | |
| 3 | 419LYS(252) | 348ARG(252) | + 38.54 | |
| 4 | 458ARG(291) | 386LYS(290) | + 7.883 | |
| 5 | 494LYS(327) | 419ARG(323) | + 39.176 | |
| 6 | 509LYS(342) | 438ARG(342) | + 4.357 | |
| 7 | 527LYS(360) | 456ARG(360) | − 2.304 | |
| 8 | 587ARG(420) | 516LYS(420) | + 43.326 | |
| 9 | 620ARG(453) | 549LYS(453) | + 76.636 | |
| 10 | 646LYS(479) | 579ARG(483) | + 4.076 | |
| 11 | 734ARG(567) | 731LYS(564) | + 23.157 | |
| 12 | 740LYS(573) | 669ARG(573) | + 19.280 | |
| 13α | 748LYS(581) | 677ARG(581) | − 23.968 | |
| 14 | 770LYS(603) | 699ARG(603) | + 73.645 | |
| 15 | 854ARG(687) | 851LYS(684) | + 92.728 | |
| 16 | 896LYS(729) | 825ARG(729) | + 55.401 | |
| 17 | 958LYS(791) | 956ARG(789) | − 2.315 | |
| 18 | 958LYS(791) | 884ARG(788) | + 65.516 | |
| 19 | 1025ARG(858) | 1022LYS(855) | + 16.130 | |
| 20 | 1055ARG(888) | 980LYS(884) | − 34.501 | |
| 21 | 1085LYS(918) | 1082ARG(915) | + 21.912 | |
| 22 | 1094ARG(927) | 1020LYS(924) | − 36.130 | |
| 23 | 1100ARG(933) | 1029LYS(933) | – | |
| 24 | 1141LYS(974) | 1073ARG(977) | + 90.852 |