TABLE 2.
Close contacts and change in solvent-accessible surface area upon peptide interaction.
| — | — | α-helical | extended | |||
|---|---|---|---|---|---|---|
| Peptide dimer | Phos. residues | Charge | Ncc | ΔΑ(Å2) | Ncc | ΔΑ(Å2) |
| P0M0 (ala)/P0M0 (ala) | 0 | +5/+5 | 1.5 | 22 | 17.4 | 274 |
| P1M2/P0M0 (ala) | 1 | +3/+5 | 42.1 | 495 | 26.1 | 332 |
| P1M2/P1M2 | 2 | +3/+3 | 29.9 | 373 | 52.0 | 632 |
| P0M0 (ace)/P2M4 | 2 | +4/0 | 33.7 | 405 | 58.6 | 762 |
| P2M4/P2M4 | 4 | 0/0 | 23.0 | 364 | 19.7 | 253 |
Notes: Phos. residues: Number of phosphorylated residues; Ncc: average number of close contacts between the two monomers in each pair, where a close contact is defined by a pair of heavy atoms being less than 4 Å apart; ΔA: excess solvent accessible surface area defined as ΔA = <A1 + A2–A12 > where A1, A2 refer to the solvent-accessible surface area of each peptidic chain considered alone and A12 refers to that of the pair. The brackets < > indicate a time average over the entire trajectory. For peptide pair annotation, see Table 1 and text.