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Related Concept Videos

Protein Folding01:25

Protein Folding

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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...
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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.
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Protein Folding Quality Check in the RER01:29

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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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Microfluidic Mixers for Studying Protein Folding
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Microfluidic Mixers for Studying Protein Folding

Published on: April 10, 2012

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Protein folding absent selection.

Thomas H Labean1, Tauseef R Butt2, Stuart A Kauffman3

  • 1Sequenomics LLC, 1428 Chanterelle Lane, Hillsborough, NC 27278, USA. labean@sequenomics.com.

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|April 9, 2014
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Summary
This summary is machine-generated.

Randomly generated protein sequences exhibit folding properties similar to biological proteins. This suggests that protein folding may be a common trait, not solely a result of evolution.

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Area of Science:

  • Biophysics
  • Molecular Biology
  • Protein Science

Background:

  • Proteins naturally fold into specific 3D structures.
  • A key question is whether this folding is due to biological selection or an inherent property of amino acid sequences.

Purpose of the Study:

  • To investigate if unevolved, random-sequence polypeptides possess structural features characteristic of biological proteins.
  • To determine if natural selection is essential for achieving compact, folded protein states.

Main Methods:

  • Expression of long (71 residue) random-sequence polypeptides.
  • Analysis of structural properties using circular dichroism and fluorescence techniques.
  • Examination of both pooled and individual protein isolates.

Main Results:

  • Prevalence of collapsed conformations in random sequences.
  • Observation of significant secondary structure formation.
  • Evidence of cooperative unfolding, similar to biological proteins.

Conclusions:

  • Compact and cooperative folded states are common in polypeptides of small protein size.
  • Natural selection is not a prerequisite for these folded states in nature.