ArticleJournal of chemical information and modeling2024
The Effect of Microwaves on Protein Structure: Molecular Dynamics Approach.
Article in Journal of chemical information and modeling, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Who cites it
9 citing papers in PubMed.
- In Vitro Antioxidant Activity and Dual-Target Inhibitory Effects of Dipyridamole on α-Amylase and α-Glucosidase: Molecular Mechanisms and Molecular Dynamics Simulations.Biomolecules · 2026Article
- Single-Frequency Microwave-Assisted Nanogel-Protein Complexation for Hybrid Biomaterial Fabrication.ACS omega · 2026Article
- Effect of Microwave on Protein Conformations and Enzymatic Reactions.Molecules (Basel, Switzerland) · 2026Review
- Comparative Study of Microwave and Ultrasound-Assisted Extraction of Phosvitin From Egg Yolk.Food science & nutrition · 2026Article
- Recent Advances in Heat-Induced Wheat Protein Modifications.Food chemistry: X · 2025Review
- Impact of Microwave Time on the Structure and Functional Properties of Glycosylated Soy 7S Globulins.Foods (Basel, Switzerland) · 2025Article
- Strategies for the drug development of cancer therapeutics.Frontiers in pharmacology · 2025Review
- Mechanism of L-arginine improving the macroscopic and microscopic qualities ofCurrent research in food science · 2025Article
- KAT6A Condensates Impair PARP1 Trapping of PARP Inhibitors in Ovarian Cancer.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2024Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
3 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The impact of microwave (MW) irradiation on protein folding, potentially inciting misfolding, was investigated by employing molecular dynamics (MD) simulations. Twenty-nine proteins were subjected to MD simulations under equilibrium (300 K) and MW conditions, where the rotational temperature was elevated to 700 K. The utilized replacement model captures the microwave effects of δ- and γ-relaxation processes (frequency range of ∼300 MHz to ∼20 GHz). The results disclosed that MW heating incited a shift toward more compact protein conformations, as indicated by decreased root-mean-square deviations, root-mean-square fluctuations, head-to-tail distances, and radii of gyration. This compaction was attributed to the intensification of intramolecular electrostatic interactions and hydrogen bonds within the protein caused by MW-destabilized hydrogen bonds between the protein and solvent. The solvent-accessible surface area (SASA), particularly that of polar amino-acid residues, shrank under MW conditions, corresponding to a reduced polarity of the water solvent. However, MW irradiation produced no significant alterations in protein secondary structures; hence, MW heating was observed to primarily affect the protein tertiary structures.
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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.