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Related Concept Videos

Protein Folding01:25

Protein Folding

7.5K
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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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.
The...
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Cotranslational Protein Translocation01:20

Cotranslational Protein Translocation

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Translocation of proteins across membranes is an ancient process that occurs even in bacteria and archaebacteria. In fact, the components of the translocation machinery are still conserved between prokaryotes and eukaryotes.
Sec61 channel partners for cotranslational translocation
During cotranslational translocation, the Sec61 channel partners with the signal recognition particle (SRP), the signal recognition particle receptor (SR), and the ribosomes to transport the nascent polypeptide chain...
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Post-translational Translocation of Proteins to the RER01:27

Post-translational Translocation of Proteins to the RER

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A sizable fraction of proteins destined for ER are first synthesized in the cell cytosol and then transported across the ER membrane–a process called post-translational translocation. Similar to cotranslationally translocated proteins, these proteins also use the Sec translocon complex to enter the ER lumen.
Targeting proteins to the ER
Hsp40 and Hsp70 chaperone molecules bind the translated proteins in the cytosol to prevent their folding. The chaperone binding helps to keep the signal...
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Proteins: From Genes to Degradation02:11

Proteins: From Genes to Degradation

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Within a biological system, the DNA encodes the RNA, and the nucleotide sequence in the RNA further defines the amino acid sequence in the protein. This is referred to as “The Central Dogma of Molecular Biology” - a term coined by Francis Crick.  Central dogma is a firm principle in biology that defines the flow of genetic information within any life form. The two fundamental steps in central dogma are - transcription and translation.
Transcription is the synthesis of RNA...
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Amyloid Fibrils03:03

Amyloid Fibrils

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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. 
Amyloid deposits were observed as early as 1639 in the liver and the spleen.   In 1854, Rudolph Virchow performed iodine staining,...
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Related Experiment Video

Updated: May 10, 2025

Analysis of Protein Folding, Transport, and Degradation in Living Cells by Radioactive Pulse Chase
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Analysis of Protein Folding, Transport, and Degradation in Living Cells by Radioactive Pulse Chase

Published on: February 12, 2019

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Cotranslational Protein Folding Through Non-Native Structural Intermediates.

Siyu Wang, Amir Bitran, Ekaterina Samatova

    Biorxiv : the Preprint Server for Biology
    |April 28, 2025
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    Summary
    This summary is machine-generated.

    Predicting protein folding during translation is difficult. This study reveals a hierarchical folding pathway stabilized by non-native interactions, offering new tools for protein design and disease research.

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    Using SecM Arrest Sequence as a Tool to Isolate Ribosome Bound Polypeptides
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    Residue-Specific Exchange of Proline by Proline Analogs in Fluorescent Proteins: How "Molecular Surgery" of the Backbone Affects Folding and Stability
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    Residue-Specific Exchange of Proline by Proline Analogs in Fluorescent Proteins: How "Molecular Surgery" of the Backbone Affects Folding and Stability

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    Area of Science:

    • Molecular Biology
    • Biophysics
    • Computational Biology

    Background:

    • Cotranslational protein folding is crucial for cellular function.
    • Misfolding due to altered translation dynamics is linked to diseases.
    • Predicting these folding pathways remains a significant challenge.

    Purpose of the Study:

    • To computationally predict and experimentally validate the vectorial hierarchy of cotranslational protein folding.
    • To investigate the role of non-native hydrophobic interactions in stabilizing early folding intermediates.
    • To understand how the chaperone Trigger Factor influences cotranslational folding.

    Main Methods:

    • Atomistic-level computational prediction of folding pathways.
    • Experimental validation of predicted folding intermediates and interactions.
    • Analysis of the impact of disrupting hydrophobic interactions on folding.
    • Investigating the effect of Trigger Factor on nascent peptide dynamics.

    Main Results:

    • A vectorial hierarchy of folding was computationally predicted and experimentally validated.
    • Early folding intermediates are stabilized by transient, non-native hydrophobic interactions.
    • Disruption of these interactions destabilizes intermediates and impairs protein folding.
    • The chaperone Trigger Factor modulates the folding pathway by maintaining peptide dynamics.

    Conclusions:

    • Surface-exposed residues play a critical role in protein folding on the ribosome.
    • The findings provide insights into the fundamental mechanisms of cotranslational folding.
    • Developed tools can improve the prediction of protein folding and aid in protein design.