ArticleScientific reports2017
Mass & secondary structure propensity of amino acids explain their mutability and evolutionary replacements.
Article in Scientific reports, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 6 papers.
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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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Who cites it
6 citing papers in PubMed.
- Predicting Supramolecular Self-Assembly of Peptide Structures with AlphaFold3.bioRxiv : the preprint server for biology · 2026Article
- Key Role of Pro230 in the Hinge Region on the Architecture and Function of IgG1.Journal of medicinal chemistry · 2026Article
- AAindexNC: Estimating the Physicochemical Properties of Non-Canonical Amino Acids, Including Those Derived from the PDB and PDBeChem Databank.International journal of molecular sciences · 2024Article
- The Evolutionary Constraints on Angiosperm Chloroplast Adaptation.Genome biology and evolution · 2023Article
- The structure of songbird MHC class I reveals antigen binding that is flexible at the N-terminus and static at the C-terminus.Frontiers in immunology · 2023Article
- In silico prediction of Severe Acute Respiratory Syndrome Coronavirus 2 main protease cleavage sites.Proteins · 2022Article
Corrections and comments
- Erratum issued
Authors and funding
3 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Why is an amino acid replacement in a protein accepted during evolution? The answer given by bioinformatics relies on the frequency of change of each amino acid by another one and the propensity of each to remain unchanged. We propose that these replacement rules are recoverable from the secondary structural trends of amino acids. A distance measure between high-resolution Ramachandran distributions reveals that structurally similar residues coincide with those found in substitution matrices such as BLOSUM: Asn ↔ Asp, P™he ↔ Tyr, Lys ↔ Arg, Gln ↔ Glu, Ile ↔ Val, Met → Leu; with Ala, Cys, His, Gly, Ser, Pro, and Thr, as structurally idiosyncratic residues. We also found a high average correlation ([Formula: see text] = 0.85) between thirty amino acid mutability scales and the mutational inertia (I
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Registered trials
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