ArticleACS central science2019
Principles of Inter-Amino-Acid Recognition Revealed by Binding Energies between Homogeneous Oligopeptides.
Article in ACS central science, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
What it found
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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
12 citing papers in PubMed.
- Validation ofACS central science · 2026Article
- Metabolic profiles and potential antioxidant mechanisms of hawk tea.Scientific reports · 2025Article
- Computational electrostatic engineering of nanobodies for enhanced SARS-CoV-2 receptor binding domain recognition.Frontiers in molecular biosciences · 2025Article
- Peptide-based coacervates in therapeutic applications.Frontiers in bioengineering and biotechnology · 2022Review
- A novel CD123-targeted therapeutic peptide loaded by micellar delivery system combats refractory acute myeloid leukemia.Journal of hematology & oncology · 2021Article
- Members of theRSC chemical biology · 2021Article
- Opposite Regulatory Effects of Immobilized Cations on the Folding Vs. Assembly of Melittin.Frontiers in chemistry · 2021Article
- Force-Field Simulations of a Hydrated Lanreotide-Based Derivative: Hydration, Dynamics, and Numerical Evidence of Self-Assembly in Dimers.ACS omega · 2020Article
- Efficient isolation and quantification of circulating tumor cells in non-small cell lung cancer patients using peptide-functionalized magnetic nanoparticles.Journal of thoracic disease · 2020Article
- Discriminating changes in protein structure using tyrosine conjugation.Protein science : a publication of the Protein Society · 2020Article
- Biomolecular Phase Separation: From Molecular Driving Forces to Macroscopic Properties.Annual review of physical chemistry · 2020Review
- Bead based facile assay for sensitive quantification of native state green fluorescent protein.RSC advances · 2020Article
Corrections and comments
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Authors and funding
21 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
We have determined the interaction strengths of the common naturally occurring amino acids using a complete binding affinity matrix of 20 × 20 pairs of homo-octapeptides consisting of the 20 common amino acids between stationary and mobile states. We used a bead-based fluorescence assay for these measurements. The results provide a basis for analyzing specificity, polymorphisms, and selectivity of inter-amino-acid interactions. Comparative analyses of the binding energies, i.e., the free energies of association (Δ
Identifiers
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Registered trials
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