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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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Molecular Chaperones and Protein Folding03:00

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Protein Folding01:22

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Protein Folding01:25

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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.
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The Unfolded Protein Response01:37

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The ER is the hub of protein synthesis in a cell. It has robust systems to quality control protein folding and also for degradation of terminally misfolded proteins. Under normal conditions, a small proportion of misfolded proteins that cannot be salvaged need to be transported to the cytoplasm by the ER-associated degradation or ERAD pathways. However, if the ERAD cannot handle the misfolded proteins, the cell activates the unfolded protein response or UPR to adjust the protein folding...
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Mechanical Protein Functions01:58

Mechanical Protein Functions

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Proteins perform many mechanical functions in a cell. These proteins can be classified into two general categories- proteins that generate mechanical forces and proteins that are subjected to mechanical forces. Proteins providing mechanical support to the structure of the cell, such as keratin, are subjected to mechanical force, whereas proteins involved in cell movement and transport of molecules across cell membranes, such as an ion pump, are examples of generating mechanical force. 
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Related Experiment Video

Updated: Jan 23, 2026

Force Spectroscopy of Single Protein Molecules Using an Atomic Force Microscope
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Force Spectroscopy of Single Protein Molecules Using an Atomic Force Microscope

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Using Single-Molecule Chemo-Mechanical Unfolding to Simultaneously Probe Multiple Structural Parameters in Protein

Emily J Guinn1, Susan Marqusee2,3,4,5

  • 1Department of Chemistry and Biochemistry, DePauw University, Greencastle, IN 46135, USA, emilyguinn@depauw.edu. emilyguinn@depauw.edu.

Methods and Protocols
|June 6, 2019
PubMed
Summary
This summary is machine-generated.

Chemo-mechanical unfolding combines force and chemical denaturants to study protein folding. This novel method probes multiple structural parameters for a deeper understanding of protein folding thermodynamics and kinetics.

Keywords:
chemo-mechanical unfoldingdenaturantforce spectroscopyoptical tweezersprotein foldingurea

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Area of Science:

  • Biophysics
  • Structural Biology
  • Biochemistry

Background:

  • Single-molecule force spectroscopy advanced protein folding studies but has limitations.
  • Studying force alone provides incomplete characterization of protein folding dynamics.

Purpose of the Study:

  • To develop and describe a novel chemo-mechanical unfolding technique.
  • To combine force and chemical denaturants for comprehensive protein folding analysis.
  • To probe multiple structural parameters simultaneously during protein folding.

Main Methods:

  • Developed chemo-mechanical unfolding, combining force and chemical denaturants.
  • Simultaneously probed changes in end-to-end distance and solvent accessible surface area.
  • Described theoretical background, experimental design, and data analysis for this technique.

Main Results:

  • The technique provides a more complete characterization of protein folding.
  • Applied to study parallel folding pathways, denatured states, and folding intermediates.
  • Enabled investigation of protein folding on the ribosome.

Conclusions:

  • Chemo-mechanical unfolding offers a powerful approach to protein folding research.
  • This method enhances the study of protein folding thermodynamics and kinetics.
  • It is applicable to diverse and complex protein folding scenarios.