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Related Concept Videos

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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Application of Monolayer Graphene to Cryo-Electron Microscopy Grids for High-resolution Structure Determination
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GRID: a high-resolution protein structure refinement algorithm.

Mohsen Chitsaz1, Stephen L Mayo

  • 1Biochemistry and Molecular Biophysics Option, California Institute of Technology, Pasadena, California 91125, USA.

Journal of Computational Chemistry
|October 16, 2012
PubMed
Summary
This summary is machine-generated.

We developed GRID, a new algorithm for refining protein structures. GRID significantly improves protein structure energy more effectively than the Backrub algorithm using similar computational resources.

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Area of Science:

  • Structural Biology
  • Computational Biology
  • Biophysics

Background:

  • Energy-based refinement of protein structures is crucial for atomic-level accuracy.
  • Accurate refinement depends on reliable force fields and efficient conformational search algorithms.

Purpose of the Study:

  • To develop and evaluate a high-resolution protein structure refinement algorithm named GRID.
  • To compare the performance of GRID against the Backrub algorithm in terms of energy improvement and computational efficiency.

Main Methods:

  • Developed the GRID algorithm for high-resolution protein structure refinement.
  • Systematically perturbed backbone dihedrals and side-chain rotamer conformations using an all-atom force field.
  • Compared GRID with the Backrub algorithm on 10 high-resolution crystal structures from the Protein Data Bank.

Main Results:

  • GRID achieved significantly better energy improvements compared to Backrub.
  • Both GRID and Backrub required similar computational resources.
  • GRID-refined structures showed slightly higher backbone RMSD (0.25 ± 0.02 Å) than Backrub (0.14 ± 0.04 Å), indicating preserved topology.

Conclusions:

  • GRID is an effective high-resolution refinement algorithm for protein structures.
  • GRID offers superior energy optimization compared to Backrub while maintaining comparable computational costs.
  • Both algorithms successfully preserve the overall topology of the refined protein structures.