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. 2021 Jun 11;8:698182. doi: 10.3389/fmolb.2021.698182

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.