Evidence map›Paper›PMID 42867160›Full record

ArticleProtein science : a publication of the Protein Society2026

MONDE·T: A database and interactive webserver for non-standard amino acids and peptide components in the PDB.

Alex Waldherr, Gesa L Freimann, Andrei N Lupas

Abstract read
In one paragraph

Article in Protein science : a publication of the Protein Society, 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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0cells of the map it votes in
0citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

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.

2 · The registry

The trial behind it

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Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

0 citing papers in PubMed.

No citing paper in PubMed yet.

4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

3 authors.

Alex WaldherrDepartment for Protein Evolution, Max Planck Institute for Biology, Tübingen, Germany.ORCID https://orcid.org/0009-0007-9721-4265
Gesa L FreimannDepartment for Protein Evolution, Max Planck Institute for Biology, Tübingen, Germany.ORCID https://orcid.org/0009-0006-4448-9831
Andrei N LupasDepartment for Protein Evolution, Max Planck Institute for Biology, Tübingen, Germany.

Funding

Max Planck Society
6 · The paper itself

Abstract

Non-standard amino acids (ncAAs) together with synthetic additions (like caps and linkers) are of wide interest for protein design and pharmaceutical optimization, as they can improve physicochemical properties and possibly reshape protein structure. Their inclusion in experimental structures has not been explored systematically. It remains elusive which components are those most impactful for protein design. We therefore collected all non-standard components present in the Protein Data Bank (PDB) into MONDE·T: A database of 1,210 unique ncAAs and 724 other synthetic components present in 23,149 PDB structures with a corresponding webserver. Analyses can focus on a single component or a single structure, illustrated here by example applications. MONDE·T allows for download of the data, visualization of a structure, identification of unusual backbone angles, and comparison of chemical similarities. The webserver is hosted at the Max Planck Institute Tübingen, accessible online via https://mondet.tuebingen.mpg.de/. MONDE·T is freely available under the Creative Commons 4.0 License.

Indexed as

Amino AcidsDatabases, ProteinPeptidesProteinsSoftwareInternetProtein ConformationAmino AcidsPeptidesProteinscell biologydatabasenon‐canonical amino acidsnon‐standard amino acidspharmaceutical optimizationpost‐translational modificationsproteinprotein designprotein structureRamachandransynthetic biologywebserver

Identifiers

PMID42867160
PMCPMC13660404

What OpenQuestion holds

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Registered trials

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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.