ReviewBiophysical reviews2020
Conformational landscape of substituted prolines.
Review in Biophysical reviews, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 31 papers.
What it found
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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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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
31 citing papers in PubMed, 67 citations in OpenAlex.
- Light-controlled inhibition of Gram-positive bacteria by photoswitchable amphiphilic lipids (PALs).RSC medicinal chemistry · 2026Article
- Nickel-Photocatalytic Deoxygenative Arylation toward β-Methyl-Branched α-Amino Acids.Organic letters · 2026Article
- Iso-pseudoprolines as versatile tools for late-stage peptide backbone modifications.Chemical science · 2026Article
- Genetic Diagnosis of Oculocutaneous Albinism Type 1A: A NovelClinical case reports · 2025Article
- Structural Adaptations of Bacterial Grx3 to Temperature: Pro29 Is Essential for Cold Adaptation inACS omega · 2025Article
- Mechanism of Cationic Peptide-Induced Assembly of Gold Nanoparticles: Modulation of Electrostatic Repulsion.Aggregate (Hoboken, N.J.) · 2025Article
- Proline isomerization modulates the bacterial IsdB/hemoglobin interaction: an atomic force spectroscopy study.Discover nano · 2025Article
- Modular Synthesis of Dehydroprolines by an Energy-Transfer Enabled Cloke-Wilson Rearrangement.Angewandte Chemie (International ed. in English) · 2025Article
- PhiSiCal-Checkup: A Bayesian framework to validate amino acid conformations within experimental protein structures.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Designing collagens to shed light on the multi-scale structure-function mapping of matrix disorders.Matrix biology plus · 2024Review
- 4-Thiaproline accelerates the slow folding phase of proteins containing cis prolines in the native state by two orders of magnitude.Protein science : a publication of the Protein Society · 2024Article
- Sodium Channel β Subunits-An Additional Element in Animal Tetrodotoxin Resistance?International journal of molecular sciences · 2024Article
- Incorporation of Aliphatic Proline Residues into Recombinantly Produced Insulin.ACS chemical biology · 2023Article
- Clickable Polyprolines from Azido-prolineACS polymers Au · 2023Article
- Discovery and pharmacophoric characterization of chemokine network inhibitors using phage-display, saturation mutagenesis and computational modelling.Nature communications · 2023Article
- Copper catalyzed Shono-type oxidation of proline residues in peptide.Science advances · 2023Article
- Conformationally constrained cyclic grafted peptidomimetics targeting protein-protein interactions.Peptide science (Hoboken, N.J.) · 2023Article
- Supramolecular Self-Assembly of Engineered Polyproline Helices.ACS macro letters · 2023Article
- Structure-Based Design of Glycosylated Oxytocin Analogues with Improved Selectivity and Antinociceptive Activity.ACS medicinal chemistry letters · 2023Article
- Novel Insights into Factor D Inhibition.International journal of molecular sciences · 2022Review
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The cyclic side chain of the amino acid proline confers unique conformational restraints on its backbone and side chain dihedral angles. This affects two equilibria-one at the backbone (cis/trans) and the other at the side chain (endo/exo). Substitutions on the proline ring impose additional steric and stereoelectronic effects that can further modulate both these equilibria, which in turn can also affect the backbone dihedral angle (ϕ, ψ) preferences. In this review, we have explored the conformational landscape of several termini capped mono-(2-, 3-, 4-, and 5-) substituted proline derivatives in the Cambridge Structural Database, correlating observed conformations with the nature of substituents and deciphering the underlying interactions for the observed structural biases. The impact of incorporating these derivatives within model peptides and proteins are also discussed for selected cases. Several of these substituents have been used to introduce bioorthogonal functionality and modulate structure-specific ligand recognition or used as spectroscopic probes. The incorporation of these diversely applicable functional groups, coupled with their ability to define an amino acid conformation via stereoelectronic effects, have a broad appeal among chemical biologists, molecular biophysicists, and medicinal chemists.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.