Editing PPIIMoL (section)

== Reference figures ==
Below are reference figures illustrating PPII bundle organization and residue patterns, reproduced with permission from Segura Rodríguez & Laurents (2024).

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File:PPIIMoL Fig1.jpg|alt=Four panels showing polyproline motifs and packing diagrams.|'''Figure 1.''' Overview of polyproline motifs.<br><small>Reproduced with permission from Segura Rodríguez & Laurents (2024).</small>
File:PPIIMoL Fig8.jpg|alt=Pie charts summarizing glycine content and flanking residues across PPII bundles.|'''Figure 8. Quantitative trends:'''<br>(A) Glycine content per PPII helix increases with number of neighbors.<br>(B) Flanking segments enriched in small polar/turn-forming residues; cationic residues often near C-termini.<br><small>Reproduced with permission from Segura Rodríguez & Laurents (2024).</small>
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File:PPIIMoL Fig2.jpg|alt=HhAFP with six PPII helices arranged in two antiparallel layers and disulfides.|'''Figure 2.''' Snow flea antifreeze protein (HhAFP): six PPII helices in two layers, stabilized by disulfides and predominantly antiparallel.<br><small>Reproduced with permission from Segura Rodríguez & Laurents (2024).</small>
File:PPIIMoL Fig3.jpg|alt=GrAFP nine-helix PPII bundle in two layers.|'''Figure 3.''' Granisotoma rainieri antifreeze protein (GrAFP): nine-helix PPII bundle arranged in two layers.<br><small>Reproduced with permission from Segura Rodríguez & Laurents (2024).</small>
File:PPIIMoL Fig4.jpg|alt=Obg GTPase domain with six PPII helices connected by variable segments.|'''Figure 4.''' Obg GTPase PPII domain: six PPII helices in two layers connected by variable segments.<br><small>Reproduced with permission from Segura Rodríguez & Laurents (2024).</small>
File:PPIIMoL Fig5.jpg|alt=Carboxylases forming compact bundles of short PPII helices.|'''Figure 5.''' Carboxylases: compact bundles of short PPII helices; one helix surrounded by six neighbors; bundle largely buried.<br><small>Reproduced with permission from Segura Rodríguez & Laurents (2024).</small>
File:PPIIMoL Fig6.jpg|alt=Bacteriophage S16 tail fiber tip with ten PPII helices and variable loops.|'''Figure 6.''' Bacteriophage S16 tail fiber tip (gp38): ten PPII helices; two fully glycine and fully surrounded; variable loops control host recognition.<br><small>Reproduced with permission from Segura Rodríguez & Laurents (2024).</small>
File:PPIIMoL Fig7.jpg|alt=Human ALK extracellular glycine-rich domain with fourteen PPII helices.|'''Figure 7.''' Human ALK extracellular glycine-rich domain: fourteen PPII helices; three nearly all-Gly; connectors range from short turns to longer elements.<br><small>Reproduced with permission from Segura Rodríguez & Laurents (2024).</small>
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