ArticleEuropean biophysics journal : EBJ2013
Overestimated accuracy of circular dichroism in determining protein secondary structure.
Article in European biophysics journal : EBJ, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. It has been retracted, and should not be counted. Cited by 7 papers.
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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.
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Who cites it
7 citing papers in PubMed, 12 citations in OpenAlex.
- Spectroscopic Analysis of the Effect of Ibuprofen Degradation Products on the Interaction between Ibuprofen and Human Serum Albumin.Current protein & peptide science · 2024Article
- Systematic FTIR Spectroscopy Study of the Secondary Structure Changes in Human Serum Albumin under Various Denaturation Conditions.Biomolecules · 2019Article
- Study of specific nanoenvironments containing α-helices in all-α and (α+β)+(α/β) proteins.PloS one · 2018Article
- An overview of osteocalcin progress.Journal of bone and mineral metabolism · 2016Review
- A new criterion to evaluate water vapor interference in protein secondary structural analysis by FTIR spectroscopy.International journal of molecular sciences · 2014Article
- Electron paramagnetic resonance spectroscopy of nitroxide-labeled calmodulin.The protein journal · 2014Article
- X-ray crystal structure of bovine 3 Glu-osteocalcin.Biochemistry · 2013Article
Corrections and comments
- Retraction · 2014-03-14Error in Data · Error in Methods · Investigation by Company/Institution · Unreliable Data · Unreliable Results and/or Conclusions ·
- Retracted
Authors and funding
5 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Circular dichroism (CD) is a spectroscopic technique widely used for estimating protein secondary structures in aqueous solution, but its accuracy has been doubted in recent work. In the present paper, the contents of nine globular proteins with known secondary structures were determined by CD spectroscopy and Fourier transform infrared spectroscopy (FTIR) in aqueous solution. A large deviation was found between the CD spectra and X-ray data, even when the experimental conditions were optimized. The content determined by FTIR was in good agreement with the X-ray crystallography data. Therefore, CD spectra are not recommended for directly calculating the content of a protein's secondary structure.
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