The DOI matches its Crossref record; 1 of the 1 references it cites were found in a registry or an index.
Quantum Chemical Profiling of Protein Mutations via Fragment-Based DFT
Open accessPreprint — published as 10.3389/fmolb.2026.1770157 · Paper page
Abstract
Missense mutations have been extensively studied in tumor-suppressing antigens (TP53) to understand oncogenesis within malignant epithelial cells. Using Whole Exome Sequencing (WXS), missense mutations can be profiled into protein sequences to identify the most common variants in tumor samples. Since nearly 80% of mutations arise randomly, it is necessary to isolate those that produce dysfunctional proteins within large cohorts. Using threading and generative algorithms such as AlphaFold and ColabFold, large cohorts of WXS information can be converted into computationally analyzable structures. By evaluating both highand low-confidence regions in these structures, these antigens can be studied en masse using pipelines that generate analytical inputs for quantum chemistry analysis. we created a pipeline that processed whole-exome sequencing (WXS) data and selected 28 representative TP53 missense mutants from the TCGA-BRCA cohort for quantum-chemical feasibility analysis. These structures were systematically cleaned using tools such as OpenBabel and AmberTools, and each was prepared for Natural Population Analysis (NPA), Electrostatic Potential (ESP) calculations, and Highest and Lowest Occupied Molecular Orbital (HOMO/LUMO) evaluation within Q-Chem. Using this pipeline, population genomics can be integrated with chemoinformatics to analyze electron density concentrations and generate hypothesis-generating electronic descriptors associated with protein dysfunction. By modifying the generated inputs, additional analyses such as Fukui orbitals, chemical shifts, and Raman shifts can also be performed. This provides a computational means to probe electronic properties not readily accessible at scale using experimental techniques.
Overview
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Integrity signals
Registry
Cites
Statistics
Figures










Verification
Claims the paper makes
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Citations
Cites
Highly accurate protein structure prediction with AlphaFold
Jumper, J., Evans, R., Pritzel, A., Green, T., Figurnov, M., Ronneberger, O., Tunyasuvunakool, K., Bates, R., Žídek, A., Potapenko, A., et al. (2021) · Nature · doi:10.1038/s41586-021-03819-2 · Cited by 43,764
Research works printed but not linked: 28
- 10.1126/science.8023157 · DOI · Paper page
- 10.1038/onc.2008.206 · DOI
- 10.1038/35094077 · DOI · Paper page
- 10.1016/j.cell.2017.08.028 · DOI · Paper page
- 10.1038/s41588-018-0204-y · DOI · Paper page
- 10.1126/science.8023159 · DOI · Paper page
- 10.1016/S0014-5793(96)01231-8 · DOI
- 10.1128/MCB.14.8.5182 · DOI · Paper page
- 10.1016/j.trecan.2025.04.003 · DOI
- 10.1111/j.1471-4159.2005.03400.x · DOI
- 10.1371/journal.pbio.0040027 · DOI · Paper page
- 10.1371/journal.pbio.0040027 · DOI · Paper page
- Kussie, P. H. , et al. “Structure of the MDM2 Oncoprotein Bound to the P53 Tumor Suppressor Transactivation Domain.” Science, 1996, pp. 948–953. · DOI · Paper page
- 10.1016/j.bbrc.2005.03.186 · DOI
- 10.1016/j.tibs.2024.10.009 · DOI
- 10.1016/S0040-4039(01)90461-7 · DOI · Paper page
- 10.1126/science.239.4839.487 · DOI · Paper page
- 10.1016/B978-0-12-418687-3.00019-7 · DOI
- 10.1038/s41467-025-57269-9 · DOI
- 10.1101/2021.10.04.463034 · DOI · Paper page
- 2022, ColabFold: Making Protein Folding Accessible to All, Nature Methods, 19, 679, 10.1038/s41592-022-01488-1 · doi:10.1038/s41592-022-01488-1 · Paper page
- 10.1038/s41586-019-1923-7 · DOI · Paper page
- 10.1093/NAR/GKAB1061 · DOI · Paper page
- 2021, Software for the Frontiers of Quantum Chemistry: An Overview of the Q-Chem 5 Package, J. Chem. Phys, 155, 084801, 10.1063/5.0055522 · DOI · Paper page
- 2006, Advances in Methods and Algorithms in a Modern Quantum Chemistry Program, PCCP, 8, 3172, 10.1039/B517914A · DOI · Paper page
- Helgaker, Trygve , Poul Jørgensen , and Jeppe Olsen . Molecular Electronic-Structure Theory. Wiley, 2000. · DOI · Paper page
- Parr, Robert G. , and Weitao Yang . Density-Functional Theory of Atoms and Molecules. Oxford University Press, 1989.
- 10.1101/cshperspect.a026195 · DOI
Metadata
- Authors
- Leyva, A., & Niazi, M. K. K.
- Affiliations
- The Ohio State University (US)
- Corresponding author
- Leyva, Alejandro
- Niazi, M. Khalid Khan
- Venue
- Frontiers in Molecular Biosciences
- Publisher
- openRxiv
- Published
- 2025-12-19
- Volume
- 13
- Pages
- 1770157-1770157
- ISSN
- 2296-889X (ISSN-L)
- PMC
- PMC12956648
- OpenAlex
- W7130308454
- Cited by
- 0
- References
- 1
- FWCI
- 0.00
- Type
- journal article
- Language
- en
- Open access
- gold
- doi.org
- Licence
- Locations
- Frontiers in Molecular Biosciences (publishedVersion, cc-by)
- bioRxiv (Cold Spring Harbor Laboratory) (acceptedVersion, cc-by)
- PubMed (publishedVersion)
- PubMed Central (publishedVersion, cc-by)
- DOAJ (DOAJ: Directory of Open Access Journals) (submittedVersion, cc-by-sa)
- Funders
- National Cancer Institute (R01CA276301)
- Topics
- Physical Sciences › Physics and Astronomy › Atomic and Molecular Physics, and Optics › Advanced Chemical Physics Studies
- Life Sciences › Pharmacology, Toxicology and Pharmaceutics › Drug Discovery › Computational Drug Discovery Methods
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Structure and Dynamics
- Keywords
- TP53, missense mutations, tumor suppressor proteins, protein dysfunction, natural population analysis, electrostatic potential, HOMO-LUMO analysis, electronic descriptors, TCGA-BRCA, protein structure prediction, cheminformatics, population genomics
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review
How to cite
Cite CoChat for the checks on this page, and the paper for its own findings.
- This page
- CoChat. (2026). Citation check: Quantum Chemical Profiling of Protein Mutations via Fragment-Based DFT. https://app.cochat.ai/papers/10.64898/2025.12.17.694938
- The paper
- Leyva, A., & Niazi, M. K. K. (2025). Quantum Chemical Profiling of Protein Mutations via Fragment-Based DFT. Frontiers in Molecular Biosciences. https://doi.org/10.64898/2025.12.17.694938
Data sources
Bibliographic data: Semantic Scholar, OpenAlex, Crossref.
Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.