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Protein Folding Quality Check in the RER01:29

Protein Folding Quality Check in the RER

ER is the primary site for the maturation and folding of soluble and transmembrane secretory proteins. The calnexin cycle is a specific chaperone system that folds and assesses the confirmation of N-glycosylated proteins before they can exit the ER lumen. The primary players of this quality check pipeline are the lectins, ER-resident chaperones, and a glucosyl transferase enzyme. In case the calnexin system in the lumen fails to salvage a misfolded protein, it is transported to the cytoplasm...

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Related Experiment Video

Updated: May 17, 2026

Deep Proteome Profiling by Isobaric Labeling, Extensive Liquid Chromatography, Mass Spectrometry, and Software-assisted Quantification
10:37

Deep Proteome Profiling by Isobaric Labeling, Extensive Liquid Chromatography, Mass Spectrometry, and Software-assisted Quantification

Published on: November 15, 2017

United3D: a protein model quality assessment program that uses two consensus based methods.

Genki Terashi1, Makoto Oosawa, Yuuki Nakamura

  • 1School of Pharmacy, Kitasato University, 5–9–1 Shirokane, Minato-ku, Tokyo 108–8641, Japan.

Chemical & Pharmaceutical Bulletin
|November 6, 2012
PubMed
Summary
This summary is machine-generated.

United3D, a new protein model quality assessment program, accurately estimates protein structure quality. It demonstrated superior performance in identifying high-quality models during the CASP9 experiment.

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A Protocol for Computer-Based Protein Structure and Function Prediction
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Last Updated: May 17, 2026

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A Protocol for Computer-Based Protein Structure and Function Prediction
16:41

A Protocol for Computer-Based Protein Structure and Function Prediction

Published on: November 3, 2011

Area of Science:

  • Computational biology
  • Structural bioinformatics
  • Protein structure prediction

Background:

  • Accurate protein model quality assessment is crucial for template-based and ab initio modeling.
  • Existing methods require robust evaluation for reliable protein structure prediction.

Purpose of the Study:

  • To develop and evaluate United3D, a novel program for automated protein model quality assessment.
  • To assess United3D's performance in identifying high-quality protein models.

Main Methods:

  • United3D utilizes an optimized clustering method and a Cα atom contact-based potential.
  • It generates quality scores (Qscore) correlated with actual model quality (GDT_TS).

Main Results:

  • United3D achieved the lowest average loss of GDT_TS (5.3) in the CASP9 experiment.
  • It showed the best performance in identifying high-quality models among tested QA methods.
  • High average Pearson (0.93) and Kendall (0.68) correlation coefficients were observed between Qscore and GDT_TS.

Conclusions:

  • United3D is a valuable tool for selecting high-quality protein models from various prediction methods.
  • The program shows competitive performance against top-ranked QA methods.
  • United3D has the potential to enhance the accuracy of protein structure prediction.