Evidence map›Paper›PMID 25205396›Full record

ArticleAnnals of biomedical engineering2014

Correlated parameter fit of arrhenius model for thermal denaturation of proteins and cells.

Zhenpeng Qin, Saravana Kumar Balasubramanian, Willem F Wolkers, John A Pearce, John C Bischof

Abstract read
In one paragraph

Article in Annals of biomedical engineering, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.

0numbers the graph read from it
0cells of the map it votes in
29citing papers in PubMed
4.0field-weighted citation impact, top 7% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

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.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

29 citing papers in PubMed, 82 citations in OpenAlex.

  1. The kinetic basis of photosynthetic heat tolerance.Nature ecology & evolution · 2026
    Article
  2. Article
  3. The Nature of Non-Arrhenius Kinetics in the Heat Denaturation of Proteins.International journal of molecular sciences · 2026
    Article
  4. Article
  5. Review
  6. Article
  7. Mathematical Descriptions of Damage to Cells and Tissues Following Heating.Advances in experimental medicine and biology · 2026
    Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Evaluation of ZnMolecules (Basel, Switzerland) · 2022
    Article
  18. Article
  19. Article
  20. Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

5 authors at 3 institutions in 2 countries.

Zhenpeng QinDepartment of Mechanical Engineering, University of Minnesota, 111 Church St. SE, Minneapolis, MN, 55455, USA.
Saravana Kumar Balasubramanian
Willem F Wolkers
John A Pearce
John C Bischof
University of Minnesota · USLeibniz University Hannover · DEThe University of Texas at Austin · US

Funding

Improved Cryosurgical Destruction of Prostate CancerR01CA075284 · NCI · UNIVERSITY OF MINNESOTA TWIN CITIES · PI BISCHOF, JOHN C · 2005 to 2009
$1.6M
NCI NIH HHS R01-CA07528NCI NIH HHS R01 CA075284
6 · The paper itself

Abstract

Thermal denaturation of proteins is critical to cell injury, food science and other biomaterial processing. For example protein denaturation correlates strongly with cell death by heating, and is increasingly of interest in focal thermal therapies of cancer and other diseases at temperatures which often exceed 50 °C. The Arrhenius model is a simple yet widely used model for both protein denaturation and cell injury. To establish the utility of the Arrhenius model for protein denaturation at 50 °C and above its sensitivities to the kinetic parameters (activation energy E a and frequency factor A) were carefully examined. We propose a simplified correlated parameter fit to the Arrhenius model by treating E a, as an independent fitting parameter and allowing A to follow dependently. The utility of the correlated parameter fit is demonstrated on thermal denaturation of proteins and cells from the literature as a validation, and new experimental measurements in our lab using FTIR spectroscopy to demonstrate broad applicability of this method. Finally, we demonstrate that the end-temperature within which the denaturation is measured is important and changes the kinetics. Specifically, higher E a and A parameters were found at low end-temperature (50 °C) and reduce as end-temperatures increase to 70 °C. This trend is consistent with Arrhenius parameters for cell injury in the literature that are significantly higher for clonogenics (45-50 °C) vs. membrane dye assays (60-70 °C). Future opportunities to monitor cell injury by spectroscopic measurement of protein denaturation are discussed.

Indexed as

Models, BiologicalProtein DenaturationCell LineCell Line, TumorCollagenHot TemperatureHumansPeptide FragmentsSerum Albumin, BovineSpectroscopy, Fourier Transform InfraredCollagenPeptide FragmentsSerum Albumin, Bovine

Identifiers

PMID25205396
PMCPMC4709256
OpenAlexW2087262377

What OpenQuestion holds

Textmetadata
LicenceTDM
Read underepoch 390

Registered trials

None linked

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.