ArticleBiopolymers2026
Polyglycine Strands Within a Collagen Triple Helix.
Article in Biopolymers, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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4 authors.
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Abstract
The collagen triple helix is the most abundant protein structural motif in animals. It tolerates any amino acid in its Xaa and Yaa positions but demands glycine (Gly) at every third position, where the residue packs into the sterically forbidding core of the triple helix and donates the recurring interstrand N-H⋯OC hydrogen bond that stitches the three strands together. (2S)-Proline (Pro) and (2S,4R)-4-hydroxyproline (Hyp) are enriched far above their proteome-wide abundance because they preorganize individual strands into the polyproline II conformation, lowering the entropic cost of folding. We asked whether the triple helix is intrinsically stable enough to form from strands that carry no such preorganization, that is, from polyglycine. To offset the conformational entropy of a Gly-rich tract, we embedded Gly
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