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Related Concept Videos

Protein Folding01:22

Protein Folding

Overview
Protein Folding01:25

Protein Folding

Proteins are chains of amino acids linked together by peptide bonds. Upon synthesis, a protein folds into a three-dimensional conformation, critical to its biological function. Interactions between its constituent amino acids guide protein folding, and hence the protein structure is primarily dependent on its amino acid sequence.
Protein Structure Is Critical to Its Biological Function
Proteins perform a wide range of biological functions such as catalyzing chemical reactions, providing...
Protein Folding01:22

Protein Folding

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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...
Molecular Chaperones and Protein Folding03:00

Molecular Chaperones and Protein Folding

The native conformation of a protein is formed by interactions between the side chains of its constituent amino acids. When the amino acids cannot form these interactions, the protein cannot fold by itself and needs chaperones. Notably, chaperones do not relay any additional information required for the folding of polypeptides; the native conformation of a protein is determined solely by its amino acid sequence. Chaperones catalyze protein folding without being a part of the folded protein.
The...
Conservation of Protein Domains Over Different Proteins02:26

Conservation of Protein Domains Over Different Proteins

Protein domains are small structurally independent units that are part of a single amino acid chain.  Although these domains are often structurally independent, they may rely on synergistic effects to perform their functions as part of a larger protein. Protein domains may be conserved within the same organism, as well as across different organisms.
A limited set of protein domains often duplicate and recombine during evolution. These domains can be organized in different combinations to form...

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Protein WISDOM: A Workbench for In silico De novo Design of BioMolecules
10:58

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Published on: July 25, 2013

Experimental optimization of protein refolding with a genetic algorithm.

Bernd Anselment1, Danae Baerend, Elisabeth Mey

  • 1Lehrstuhl für Bioverfahrenstechnik, Technische Universität München, Boltzmannstr. 15, D-85748 Garching, Germany.

Protein Science : a Publication of the Protein Society
|August 28, 2010
PubMed
Summary
This summary is machine-generated.

Optimizing protein refolding from inclusion bodies is challenging. A new strategy using a genetic algorithm (GA) efficiently screens conditions, achieving high refolding yields (74-100%) for diverse proteins.

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Coupled Assays for Monitoring Protein Refolding in Saccharomyces cerevisiae
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Published on: July 9, 2013

Area of Science:

  • Biochemistry
  • Molecular Biology
  • Protein Engineering

Background:

  • Protein refolding from solubilized inclusion bodies is a significant challenge in recombinant protein production.
  • Empirical screening of numerous parameters is typically required to determine optimal refolding conditions.

Purpose of the Study:

  • To develop a robust and universal method for optimizing protein refolding yields.
  • To combine experimental screening with a genetic algorithm (GA) for efficient optimization.

Main Methods:

  • A genetic algorithm (GA) was employed to guide the screening and optimization of protein refolding conditions.
  • A wide range of common refolding additives and conditions were incorporated into the screening process.
  • The method was tested on four structurally and functionally diverse model proteins.

Main Results:

  • The GA-guided strategy successfully optimized refolding conditions for all tested proteins.
  • Achieved refolding yields ranged from 74% to 100% across the four model proteins.
  • Optimal conditions identified by the GA also enhanced the activity of the native enzymes.

Conclusions:

  • The developed strategy offers a generally applicable and efficient approach for optimizing protein refolding.
  • This method streamlines the process, reducing the bottleneck associated with empirical refolding optimization.
  • The GA-guided approach is suitable for a wide variety of enzymes and proteins.