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Related Concept Videos

Protein Folding01:25

Protein Folding

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...
Protein Folding01:22

Protein Folding

Overview
Protein Folding01:22

Protein Folding

Overview
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...
Protein Folding Quality Check in the RER01:29

Protein Folding Quality Check in the RER

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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Related Experiment Video

Updated: Jul 8, 2026

Microfluidic Mixers for Studying Protein Folding
12:42

Microfluidic Mixers for Studying Protein Folding

Published on: April 10, 2012

Protein folding transition states probed by loop extension.

Ignacio Enrique Sánchez1

  • 1Fundacion Instituto Leloir, Buenos Aires, Argentina. isanchez@leloir.org.ar

Protein Science : a Publication of the Protein Society
|December 25, 2007
PubMed
Summary

We developed a novel method to study protein folding transition states by analyzing loop perturbations. This technique quantifies the loop

Area of Science:

  • Biochemistry and Molecular Biology
  • Protein Dynamics
  • Chemical Physics

Background:

  • Understanding protein folding transition states is crucial for deciphering protein function and misfolding diseases.
  • Current methods for characterizing transition states have limitations in resolving structural details.
  • Protein loop regions play a significant role in folding pathways but are challenging to study.

Purpose of the Study:

  • To introduce a new method, alpha(Loop), for characterizing protein folding transition states.
  • To investigate the structural implications of loop perturbations on protein folding kinetics and thermodynamics.
  • To detect residual structure in unfolded proteins using polymer theory.

Main Methods:

  • Insertion of residues into unstructured protein loops.

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Microfluidic Mixers for Studying Protein Folding
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Thermodynamics of Membrane Protein Folding Measured by Fluorescence Spectroscopy
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  • Measurement of changes in protein folding kinetics and thermodynamics.
  • Analysis using a rate-equilibrium free energy relationship, alpha(Loop).

    • Main Results:

    • The alpha(Loop) parameter quantifies the fraction of molecules with a perturbed loop in the transition state.
    • Changes in equilibrium free energy provide insights into residual structure in the unfolded state.
    • The method was successfully applied to model proteins CI2 and the alpha spectrin SH3 domain.

    Conclusions:

    • The alpha(Loop) approach offers a novel way to characterize protein folding transition states.
    • This method can reveal details about the unfolded state, including residual structure.
    • The findings contribute to a deeper understanding of protein folding mechanisms.