ArticleACS omega2022
Proteins' Evolution upon Point Mutations.
Article in ACS omega, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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Who cites it
13 citing papers in PubMed.
- Evolutionary tuning of the molecular charge state of UBP24 shapes responses to high temperature.Nature plants · 2026Article
- Exploration of genes and identification of evolutionary evidence in adeno-associated viruses.Journal of microbiology (Seoul, Korea) · 2026Article
- Factors controlling protein evolvability-at the molecular scale.European biophysics journal : EBJ · 2026Article
- Comprehensive In Silico Analysis of the CXCL12, C55Y Mutation Reveals Structural and Functional Disruption in CXCR4/CXCR7 Signaling.Evolutionary bioinformatics online · 2026Article
- Molecular Mechanisms of Venom Diversity.Toxins · 2025Review
- An AI-Designed Antibody-Engineered Probiotic Therapy Targeting Urease to CombatMicroorganisms · 2025Article
- Impact of a Heterozygous C1RCells · 2025Article
- The origin of mutational epistasis.European biophysics journal : EBJ · 2024Article
- Analysis of proteins in the light of mutations.European biophysics journal : EBJ · 2024Review
- Protein structure prediction from the complementary science perspective.Biophysical reviews · 2023Article
- Protein folding rate evolution upon mutations.Biophysical reviews · 2023Review
- Rethinking the protein folding problem from a new perspective.European biophysics journal : EBJ · 2023Article
- Conformational Stability and Denaturation Processes of Proteins Investigated by Electrophoresis under Extreme Conditions.Molecules (Basel, Switzerland) · 2022Review
Corrections and comments
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Authors and funding
1 author.
Funding
No grant is acknowledged in the PubMed record.
Abstract
As the reader must be already aware, state-of-the-art protein folding prediction methods have reached a smashing success in their goal of accurately determining the three-dimensional structures of proteins. Yet, a solution to simple problems such as the effects of protein point mutations on their (i) native conformation; (ii) marginal stability; (iii) ensemble of high-energy nativelike conformations; and (iv) metamorphism propensity and, hence, their evolvability, remains as an unsolved problem. As a plausible solution to the latter, some properties of the amide hydrogen-deuterium exchange, a highly sensitive probe of the structure, stability, and folding of proteins, are assessed from a new perspective. The preliminary results indicate that the protein marginal stability change upon point mutations provides the necessary and sufficient information to estimate, through a Boltzmann factor, the evolution of the amide hydrogen exchange protection factors and, consequently, that of the ensemble of folded conformations coexisting with the native state. This work contributes to our general understanding of the effects of point mutations on proteins and may spur significant progress in our efforts to develop methods to determine the appearance of new folds and functions accurately.
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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.