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Related Concept Videos

Molecular Chaperones and Protein Folding03:00

Molecular Chaperones and Protein Folding

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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 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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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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Globular Proteins01:27

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In organisms, proteins are the most abundant macromolecules. They act as the building blocks of life and play various crucial roles in the body. Proteins can be broadly classified into two distinct subtypes based on their shape and solubilities: globular proteins and fibrous proteins.
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Protein and Protein Structure02:15

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Proteins are one of the most abundant organic molecules in living systems and have the most diverse range of functions of all macromolecules. Proteins may be structural, regulatory, contractile, or protective. They may serve in transport, storage, or membranes; or they may be toxins or enzymes. Their structures, like their functions, vary greatly. They are all, however, amino acid polymers arranged in a linear sequence.
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Globular and Fibrous Proteins02:21

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Many proteins can be classified into two distinct subtypes - globular or fibrous. These two types differ in their shapes and solubilities.
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Single-Molecule Fluorescence Visualization of DNA Polymerase Dynamics at G-Quadruplexes
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Single-Molecule Fluorescence Visualization of DNA Polymerase Dynamics at G-Quadruplexes

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Why are G-quadruplexes good at preventing protein aggregation?

Theodore J Litberg1, Rajesh Kumar Reddy Sannapureddi2, Zijue Huang1

  • 1Department of Chemistry & Biochemistry and the Knoebel Institute for Healthy Aging, University of Denver, Denver, CO, USA.

RNA Biology
|July 26, 2023
PubMed
Summary

Nucleic acids called G-quadruplexes act as chaperones, preventing protein aggregation. Their structural topology, dynamics, and oligomerization state determine this protective holdase activity, crucial for cellular health and neurodegenerative disease insights.

Keywords:
NMRRNA and DNA structurechaperoneprotein aggregationquadruplex

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A G-quadruplex DNA-affinity Approach for Purification of Enzymatically Active G4 Resolvase1
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Area of Science:

  • Molecular Biology
  • Biochemistry
  • Structural Biology

Background:

  • Maintaining a healthy protein folding environment is critical for cellular function.
  • Protein aggregation is implicated in various diseases, including neurodegenerative disorders.
  • Nucleic acids, particularly G-quadruplexes, have emerged as potential modulators of protein aggregation.

Purpose of the Study:

  • To investigate the role of G-quadruplexes as chaperones in preventing protein aggregation.
  • To identify the key structural and dynamic factors that contribute to the holdase activity of G-quadruplexes.
  • To understand how these factors influence the G-quadruplexes' ability to prevent protein misfolding and aggregation.

Main Methods:

  • Structure-function analysis of G-quadruplex forming sequences (PARP-I and LTR-III).
  • Nuclear Magnetic Resonance (NMR) spectroscopy to analyze G-quadruplex structure and dynamics.
  • Assays to evaluate the holdase activity of G-quadruplexes in preventing protein aggregation.

Main Results:

  • G-quadruplexes were confirmed as potent chaperones against protein aggregation.
  • Three critical factors influencing G-quadruplex holdase activity were identified: structural topology, accessibility/dynamics, and oligomerization state.
  • These factors collectively determine the efficacy of G-quadruplexes in preventing the aggregation of partially misfolded proteins.

Conclusions:

  • G-quadruplexes possess significant chaperone capabilities, modulating protein aggregation.
  • The identified physical traits (topology, dynamics, oligomerization) are key determinants of G-quadruplex holdase activity.
  • Understanding these G-quadruplex properties may offer insights into therapeutic strategies for protein aggregation diseases.