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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
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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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Amyloid Fibrils03:03

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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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Defining Hsp33's Redox-regulated Chaperone Activity and Mapping Conformational Changes on Hsp33 Using Hydrogen-deuterium Exchange Mass Spectrometry
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Oxidative protein folding: nature's knotty challenge.

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Oxidative protein folding (OPF), essential for protein structure and function, involves disulfide bond formation. Dysregulation of OPF can lead to cellular stress and disease, but new insights offer therapeutic potential.

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Area of Science:

  • Biochemistry
  • Molecular Biology
  • Cellular Biology

Background:

  • Oxidative protein folding (OPF) is a fundamental post-translational modification involving intramolecular disulfide bond formation.
  • OPF is crucial for achieving the correct three-dimensional protein structure, which dictates protein function and cellular homeostasis.
  • The process is managed by specific oxidase and isomerase enzymes, addressing a complex biochemical challenge.

Discussion:

  • OPF, while essential, can paradoxically generate reactive oxygen species under cellular stress.
  • This oxidative stress contributes to endoplasmic reticulum stress, impaired protein folding, and the unfolded protein response.
  • The unfolded protein response can trigger pro-inflammatory signals linked to various diseases, including metabolic disorders, neurodegeneration, and cancer.

Key Insights:

  • Recent research highlights the intricate regulatory mechanisms governing OPF.
  • Understanding the balance between OPF and oxidative stress is critical for cellular health.
  • New findings reveal the divergent pathways involved in orchestrating OPF.

Outlook:

  • Advances in understanding OPF offer potential for novel therapeutic strategies.
  • Industrial biotechnology may benefit from improved control over protein folding processes.
  • Future research will continue to unravel the complexities of OPF and its role in health and disease.