ArticleThe journal of physical chemistry letters2012
Protein Electrostatic Properties Predefining the Level of Surface Hydrophobicity Change upon Phosphorylation.
Article in The journal of physical chemistry letters, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.
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Who cites it
21 citing papers in PubMed.
- In silico conformational dynamics of the α-actinin-2 actin-binding domain upon phosphorylation.Biophysical journal · 2026Article
- Altering the Properties of Laccases fromBiomolecules · 2025Article
- Thermal Denaturation of Fresh Frozen Tissue Enhances Mass Spectrometry Detection of Peptides.Analytical chemistry · 2024Article
- Poaceae plants transfer cyclobutane pyrimidine dimer photolyase to chloroplasts for ultraviolet-B resistance.Plant physiology · 2024Article
- Western blotting (immunoblotting): history, theory, uses, protocol and problems.BioTechniques · 2023Review
- Phosphorylation Induced Conformational Transitions in DNA PolymeraseFrontiers in molecular biosciences · 2022Article
- Molecular dynamics shows complex interplay and long-range effects of post-translational modifications in yeast protein interactions.PLoS computational biology · 2021Article
- Protein Interaction with Charged Macromolecules: From Model Polymers to Unfolded Proteins and Post-Translational Modifications.International journal of molecular sciences · 2019Review
- The Effect of FG-Nup Phosphorylation on NPC Selectivity: A One-Bead-Per-Amino-Acid Molecular Dynamics Study.International journal of molecular sciences · 2019Article
- Role of Computational Methods in Going beyond X-ray Crystallography to Explore Protein Structure and Dynamics.International journal of molecular sciences · 2018Review
- How phosphorylation influences E1 subunit pyruvate dehydrogenase: A computational study.Scientific reports · 2018Article
- Impact of Phosphorylation on the Mass Spectrometry Quantification of Intact Phosphoproteins.Analytical chemistry · 2018Article
- Phosphorylation of SNAP-23 regulates its dynamic membrane association during mast cell exocytosis.Biology open · 2017Article
- An overview of technical considerations for Western blotting applications to physiological research.Scandinavian journal of medicine & science in sports · 2017Review
- Chronic opioid treatment augments caveolin-1 scaffolding: relevance to stimulatory μ-opioid receptor adenylyl cyclase signaling.Journal of neurochemistry · 2016Article
- Comparison of phosphorylation patterns across eukaryotes by discriminative N-gram analysis.BMC bioinformatics · 2015Article
- Thermodynamics of the interaction between Alzheimer's disease related tau protein and DNA.PloS one · 2014Article
- Vienna-PTM web server: a toolkit for MD simulations of protein post-translational modifications.Nucleic acids research · 2013Article
- Modular organization of α-toxins from scorpion venom mirrors domain structure of their targets, sodium channels.The Journal of biological chemistry · 2013Article
- A systematic framework for molecular dynamics simulations of protein post-translational modifications.PLoS computational biology · 2013Article
Corrections and comments
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Authors and funding
2 authors.
Funding
Abstract
We use explicit-solvent, molecular dynamics simulations to study the change in polar properties of a solvent-accessible surface for proteins undergoing phosphorylation. We analyze eight different pairs of proteins representing different structural classes in native and phosphorylated states and estimate the polarity of their surface using the molecular hydrophobicity potential approach. Whereas the phosphorylation-induced hydrophobicity change in the vicinity of phosphosites does not vary strongly among the studied proteins, the equivalent change for complete proteins covers a surprisingly wide range of effects including even an increase in the overall hydrophobicity in some cases. Importantly, the observed changes are strongly related to electrostatic properties of proteins, such as the net charge per residue, the distribution of charged side-chain contacts, and the isoelectric point. These features predefine the level of surface hydrophobicity change upon phosphorylation and may thus contribute to the phosphorylation-induced alteration of the interactions between a protein and its environment.
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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.