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Protein Folding01:22

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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.
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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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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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Amyloid fibrils are aggregates of misfolded proteins.  Under most circumstances, misfolded proteins are either refolded by chaperone proteins or degraded by the proteasome. However, in the case of a mutation or a disease, these proteins can accumulate to form large clusters and often further assemble to form elongated fibers, called fibrils. 
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Related Experiment Video

Updated: Feb 5, 2026

Microfluidic Mixers for Studying Protein Folding
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Published on: April 10, 2012

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What's in the "fold"?

Parul Mehra1, Anuradha Kalani2

  • 1Diabetes and Obesity Center, Department of Cardiovascular Medicine, University of Louisville, Louisville, KY 40202, USA; Children's Hospital of Philadelphia, Department of Pathology and Laboratory Medicine, Abramson Research Center, 3516 Civic Center Boulevard, Philadelphia PA-19104, USA.

Life Sciences
|September 15, 2018
PubMed
Summary
This summary is machine-generated.

Genome architecture and 3D chromatin folding are crucial for gene regulation and cell function. Understanding these complex structures is key to deciphering healthy and diseased states.

Keywords:
CTCFCancerChromatin loopingChromosome Conformation Capture (3C)CohesinHi-CHigher order chromatin architecturePcGSuper enhancersTopologically Associated Domains

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Area of Science:

  • Genomics
  • Epigenetics
  • Molecular Biology

Background:

  • Genome architecture dictates gene expression from development to adult phenotypes.
  • Hierarchical genome organization influences cell functions like X-chromosome inactivation and DNA repair.
  • Chromatin loops and topologically-associated domains form basic units of genome organization.

Purpose of the Study:

  • To explore the principles of spatial and regulatory relationships in 3D chromatin landscapes.
  • To investigate the impact of chromatin folding on genome structure and function.
  • To understand how altered chromatin folding affects genome function in health and disease.

Main Methods:

  • Review of current literature on genome architecture and 3D chromatin organization.
  • Analysis of principles governing spatial and regulatory genome interactions.
  • Discussion of the link between chromatin folding and gene regulation.

Main Results:

  • 3D chromatin folding creates complex networks, forming compartments and territories.
  • Changes in chromatin folding significantly influence genome function.
  • Understanding these mechanisms is vital for comprehending human diseases.

Conclusions:

  • The spatial organization of the genome is fundamental to its function.
  • Altered 3D chromatin folding is implicated in various diseases.
  • Further research into "what's in the fold" is essential for medical advancements.