ReviewAmino acids2024
Proline, a unique amino acid whose polymer, polyproline II helix, and its analogues are involved in many biological processes: a review.
Review in Amino acids, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.
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17 citing papers in PubMed.
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- Structure determination and dual targeting of a plant TACO1 identifies its ancient role as an organelle translation regulator.bioRxiv : the preprint server for biology · 2026Article
- Beyond osmoprotection: the expanding roles of proline in plant signalling and development.Biologia futura · 2026Review
- Conformational Switching Controls Biradical Spin Dynamics in Flavin-Tryptophan Dyads.Journal of the American Chemical Society · 2026Article
- Inflammation suppressing activity of jellyfish toxin-derived peptide via downregulation of ROS/NF-κB/NLRP3 signaling in LPS/MSU induced fibroblasts in vitro and in vivo gouty arthritis model.Inflammopharmacology · 2026Article
- Assessment of Energy Effects DeterminingACS physical chemistry Au · 2026Article
- Synthesis, characterization, and anticancer activity of tuna bone gelatin peptide-stabilized selenium nanowires.RSC advances · 2025Article
- Mutations in the Esx-3 secretion system confer resistance to multiple chemical scaffolds inMicrobiology (Reading, England) · 2025Article
- An Evolutionary Study in Glyphosate Oxidoreductase Gox Highlights Distinct Orthologous Groups and Novel Conserved Motifs That Can Classify Gox and Elucidate Its Biological Role.Journal of xenobiotics · 2025Article
- Origin-Dependent Molecular Ordering in Gelatin and Its Impact on Electrospun Nanofiber.Polymers · 2025Article
- The Spliceosomal Peptidyl Prolyl Isomerase Like 1 Interacts with the Low-Complexity Domain of the RNA Binding Protein EWS Modulating Its Phase Separation Behavior.Biochemistry · 2025Article
- Tracing the Evolutionary Expansion of a Hyperdiverse Antimicrobial Peptide Gene Family inGenes · 2025Article
- Timbe (Pharmaceuticals (Basel, Switzerland) · 2025Article
- Article
- MODY PDX1Frontiers in endocrinology · 2025Article
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7 authors.
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Abstract
Proline is a unique amino acid in that its side-chain is cyclised to the backbone, thus giving proline an exceptional rigidity and a considerably restricted conformational space. Polyproline forms two well-characterized helical structures: a left-handed polyproline helix (PPII) and a right-handed polyproline helix (PPI). Usually, sequences made only of prolyl residues are in PPII conformation, but even sequences not rich in proline but which are rich in glycine, lysine, glutamate, or aspartate have also a tendency to form PPII helices. Currently, the only way to study unambiguously PPII structure in solution is to use spectroscopies based on optical activity such as circular dichroism, vibrational circular dichroism and Raman optical activity. The importance of the PPII structure is emphasized by its ubiquitous presence in different organisms from yeast to human beings where proline-rich motifs and their binding domains are believed to be involved in vital biological processes. Some of the domains that are bound by proline-rich motifs include SH3 domains, WW domains, GYF domains and UEV domains, etc. The PPII structure has been demonstrated to be essential to biological activities such as signal transduction, transcription, cell motility, and immune response.
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