Electric field effects on insulin chain-B conformation.

The journal of physical chemistry. B · 2005 · Mixed · Very low evidence

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MixedVery low evidencePaper 3559

Molecular dynamics simulations indicated that both static and oscillating electric fields (10^7 to 10^9 V/m) altered insulin chain-B behavior. Oscillating fields were reported as more disruptive to structure than static fields of similar effective strength, w…

Study snapshot

PublicationThe journal of physical chemistry. B · 2005
Study typein_vitro
Reported directionMixed
Evidence ratingVery low

Abstract

The response of proteins to different forms of stress continues to be a topic of major interest, especially with the proliferation of electromagnetic devices conjectured to have detrimental effects on human health. In this paper, we have performed molecular dynamics simulations on insulin chain-B under the influence of both static and oscillating electric fields, ranging from 10(7) to 10(9) V/m. We have found that both variants have an effect on the normal behavior of the protein, with oscillating fields being more disruptive to the structure as compared to static fields of similar effective strength. The application of a static field had a stabilizing effect on the secondary structure, restricting the inherent flexibility that is crucial for insulin's biological activity.

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AI evidence extraction

Structured fields below were generated from the paper’s abstract and metadata to make the evidence easier to inspect. Automated extraction may be incomplete or incorrect; verify important details against the original paper.

Study typein_vitro
Effect directionmixed
PopulationNot supplied
Sample sizeNot supplied
ExposureNot supplied
Evidence strengthVery lowConfidence: 74% · Peer reviewed: yes

Main findings

Molecular dynamics simulations indicated that both static and oscillating electric fields (10^7 to 10^9 V/m) altered insulin chain-B behavior. Oscillating fields were reported as more disruptive to structure than static fields of similar effective strength, while static fields stabilized secondary structure and restricted flexibility important for biological activity.

Outcomes measured

  • Insulin chain-B conformation/structure
  • Secondary structure stability
  • Protein flexibility (molecular dynamics behavior)

Limitations

  • Simulation study (molecular dynamics) rather than measurements in biological systems
  • No exposure frequency specified for oscillating fields in the abstract
  • No exposure duration reported in the abstract
View raw extracted JSON
{
  "study_type": "in_vitro",
  "exposure": {
    "band": null,
    "source": "electric field (static and oscillating)",
    "frequency_mhz": null,
    "sar_wkg": null,
    "duration": null
  },
  "population": null,
  "sample_size": null,
  "outcomes": [
    "Insulin chain-B conformation/structure",
    "Secondary structure stability",
    "Protein flexibility (molecular dynamics behavior)"
  ],
  "main_findings": "Molecular dynamics simulations indicated that both static and oscillating electric fields (10^7 to 10^9 V/m) altered insulin chain-B behavior. Oscillating fields were reported as more disruptive to structure than static fields of similar effective strength, while static fields stabilized secondary structure and restricted flexibility important for biological activity.",
  "effect_direction": "mixed",
  "limitations": [
    "Simulation study (molecular dynamics) rather than measurements in biological systems",
    "No exposure frequency specified for oscillating fields in the abstract",
    "No exposure duration reported in the abstract"
  ],
  "evidence_strength": "very_low",
  "confidence": 0.74,
  "peer_reviewed_likely": "yes",
  "keywords": [
    "electric field",
    "static field",
    "oscillating field",
    "molecular dynamics",
    "insulin chain-B",
    "protein conformation",
    "secondary structure",
    "protein flexibility"
  ],
  "suggested_hubs": []
}
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AI-extracted fields are generated from the abstract and metadata and may be incomplete or incorrect. This material is for informational purposes and is not medical advice.

Identifiers and source

DOI: 10.1021/jp052742q
PubMed: 16853947

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