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Related Concept Videos

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...
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...
Clot Retraction and Fibrinolysis01:16

Clot Retraction and Fibrinolysis

After a fibrin clot is formed, the next step is clot retraction, a vital process facilitated by platelet contractile proteins, such as actin and myosin. These proteins pull the fibrin strands closer together and condense the clot. This action reduces the size of the clot, creating a smaller, denser structure that effectively seals off the damaged vessel. Clot retraction consolidates the clot and helps with wound healing by bringing the edges of the damaged blood vessel closer together.
Amyloid Fibrils03:03

Amyloid Fibrils

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. 
Amyloid deposits were observed as early as 1639 in the liver and the spleen.   In 1854, Rudolph Virchow performed iodine staining, normally used to...
Fibril-associated Collagen01:11

Fibril-associated Collagen

Fibril-associated collagens are a type of collagens present in the extracellular matrix with interrupted triple helices or FACIT (Fibril-associated collagens interrupted triple-helices). FACIT help connect and attach the collagen fibrils with each other as well as with other proteins of the extracellular matrix.
For example, the type II collagen fibrils in cartilage have covalently bound type IX fibril-associated collagens at regular intervals. Other types of fibril-associated collagens are...
Bacterial Protein Maturation01:26

Bacterial Protein Maturation

Bacterial protein maturation is a tightly regulated process that ensures newly synthesized polypeptides achieve correct functional conformations. This maturation involves a series of modifications, folding events, and quality control steps, often assisted by specialized chaperone proteins.N-Terminal ModificationsThe maturation of bacterial polypeptides begins cotranslationally as the polypeptide exits the ribosome. The first amino acid, N-formylmethionine (fMet), is typically modified at the...

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Analysis of β-Amyloid-induced Abnormalities on Fibrin Clot Structure by Spectroscopy and Scanning Electron Microscopy
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Fibrinogen has chaperone-like activity.

Huadong Tang1, Yan Fu, Yujie Cui

  • 1National Engineering Laboratory for Anti-tumor Protein Therapeutics Tsinghua University, Beijing 100084, China.

Biochemical and Biophysical Research Communications
|December 9, 2008
PubMed
Summary
This summary is machine-generated.

Fibrinogen, an abundant extracellular protein, exhibits chaperone-like activity. It prevents thermal aggregation and aids refolding of other proteins, suggesting a novel role in cellular protection and potential therapeutic applications.

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Experimental and Imaging Techniques for Examining Fibrin Clot Structures in Normal and Diseased States
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Experimental and Imaging Techniques for Examining Fibrin Clot Structures in Normal and Diseased States

Published on: April 1, 2015

Area of Science:

  • Biochemistry
  • Molecular Biology
  • Protein Chemistry

Background:

  • Partially unfolded proteins aggregate via hydrophobic interactions.
  • Extracellular protein stress responses and chaperone roles are understudied.

Purpose of the Study:

  • To investigate the potential chaperone-like activity of fibrinogen.
  • To explore fibrinogen's role in preventing protein aggregation in extracellular environments.

Main Methods:

  • Assessing fibrinogen's effect on thermal aggregation and inactivation of citrate synthase.
  • Evaluating fibrinogen's ability to maintain luciferase in a refolding-competent state.
  • Observing fibrinogen's impact on yeast prion protein (Sup35 NM) fibril formation.
  • Testing fibrinogen's efficacy in rescuing thermal-induced protein aggregation in mouse plasma.

Main Results:

  • Fibrinogen specifically binds to nonnative citrate synthase, inhibiting its aggregation and inactivation independently of ATP.
  • Fibrinogen preserves thermal-denatured luciferase, enabling subsequent refolding.
  • Fibrinogen inhibits the aggregation of yeast prion protein Sup35 (NM).
  • Fibrinogen administration rescues thermal protein aggregation in fibrinogen-deficient mouse plasma.

Conclusions:

  • Fibrinogen possesses significant chaperone-like activity.
  • This finding expands understanding of extracellular chaperone systems.
  • Fibrinogen's activity suggests potential diagnostic and therapeutic strategies for related conditions.