Molecular Unfolding
Molecular Unfolding - Related Videos
01:37
The Unfolded Protein Response
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2023
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...
02:38
Assessing Bacterial Chaperone Activity via Thermal Unfolding of a Model Protein
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2025
Source: Dahl, J. et al. Detection of the pH-dependent Activity of Escherichia coli Chaperone HdeB In Vitro and In Vivo. J. Vis. Exp. (2016)This video demonstrates a fluorescence spectrophotometer-based assay to evaluate chaperone activity on a substrate protein under acid and heat stress. It outlines the steps for monitoring substrate unfolding and aggregation through light scattering, comparing conditions with and without the chaperone.
03:25
Recording Neural Activity of Unfolded Hippocampal Tissue Using Penetrating Microelectrode Array
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2025
This video demonstrates the procedure to set up a recording chamber with a penetrating microelectrode array (PMEA) to capture neural signals from an unfolded hippocampus. This method allows us to study the speed and direction of propagation of neural activity within the unfolded hippocampus in vitro.
09:48
Neural Activity Propagation in an Unfolded Hippocampal Preparation with a Penetrating Micro-electrode Array
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Cited by 2 •
2015
We have developed an in vitro unfolded hippocampus which preserves CA1-CA3 array of neurons. Combined with the penetrating micro-electrode array, neural activity can be monitored in both the longitudinal and transverse orientations. This method provides advantages over hippocampal slice preparations as the propagation in the entire hippocampus can be recorded simultaneously.
03:00
Molecular Chaperones and Protein Folding
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2020
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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Molecular unfolding begins when stabilizing interactions no longer collectively maintain the native arrangement. Hydrogen bonds, hydrophobic interactions, and other forces can each contribute to resistance, but their relative influence depends on the molecule and surrounding conditions. As these interactions weaken, the chain can access more extended conformations, helping explain both loss of function and emergence of altered physical behavior.
Heat, pH changes, chemical denaturants, and mechanical force can all drive unfolding by weakening the interactions that stabilize a protein's three-dimensional structure. These triggers represent different environmental or physical stresses, yet they can produce a shared shift toward less ordered conformations. Comparing responses across stresses helps reveal how molecular stability depends on external conditions.
A molecule's sequence and its environment jointly influence how readily its structure changes. Sequence determines the interactions available within the polypeptide chain, while environmental conditions can weaken those interactions and alter the balance between folded and extended conformations. Studying both factors helps bioengineers connect molecular structure with stability, function, and stress response.
These techniques provide complementary evidence about structural transitions. Spectroscopy can monitor molecular changes associated with altered structure, calorimetry examines behavior during thermal perturbation, and single-molecule force measurements assess responses to mechanical stress. Together, they help researchers determine how stability changes under different conditions and connect molecular-scale transitions with measurable physical outcomes.
Bioengineers study unfolding to measure molecular stability and to guide the design of more resilient enzymes and therapeutic proteins. The same analysis can show how sequence and environmental stress affect function, allowing researchers to evaluate whether a molecule remains structurally useful under challenging conditions. These insights support the development and characterization of engineered biological materials.
Unfolding studies show how structural disruption can create new physical properties and contribute to aggregation-related disease mechanisms. They also help characterize biomaterials whose performance depends on molecular structure and stress response. By measuring transitions rather than examining function alone, researchers can connect changes in conformation with material behavior or disease-relevant aggregation processes.