Mechanical Unfolding
Mechanical Unfolding - Related Videos
01:37
The Unfolded Protein Response
0 Views •
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...
09:48
Neural Activity Propagation in an Unfolded Hippocampal Preparation with a Penetrating Micro-electrode Array
0 Views •
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.
02:38
Assessing Bacterial Chaperone Activity via Thermal Unfolding of a Model Protein
0 Views •
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
0 Views •
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.
01:31
Regulation of the Unfolded Protein Response
0 Views •
2023
Inositol-requiring kinase one or IRE1 is the most conserved eukaryotic unfolded protein response (UPR) receptor. It is a type I transmembrane protein kinase receptor with a distinctive site-specific RNase activity. As the binding mechanics of the misfolded proteins with the N-terminal domain of IRE-1 are unclear, three binding models — direct, indirect, and allosteric -- are proposed for receptor activation. Nevertheless, it is known that once a misfolded protein associates with IRE1, it...
FAQs
Force–extension profiles show how molecular extension changes as applied tension increases. Distinct changes in the profile can indicate successive structural transitions rather than a single, uninterrupted disruption. By examining these patterns, researchers can identify unfolding events and relate them to the molecule’s response to physical stress, providing a more detailed view of its mechanical behavior.
Atomic force microscopy and optical tweezers provide ways to apply controlled tension to individual molecules. The experiment depends on attaching the molecule at defined molecular attachment points, then monitoring force and extension as tension changes. Using these tools, researchers can connect externally applied mechanical stress with structural transitions and quantify how biomolecules respond.
Refolding behavior adds information beyond the force required to disrupt a folded structure. If a molecule shows refolding after tension changes, the observation indicates that its structural response can include reversible behavior under the tested conditions. This helps researchers characterize molecular stability and distinguish unfolding-related responses from measurements that only capture disruption.
A typical workflow attaches an individual molecule to the measurement system, applies controlled tension with atomic force microscopy or optical tweezers, and records force together with molecular extension. Researchers then inspect the resulting force–extension profile for structural transitions, unfolding events, and possible refolding. These measurements convert molecular responses to stress into interpretable mechanical data.
Measurements of force, extension, and structural transitions provide quantitative information about molecular stability under mechanical stress. Bioengineers can use these results to compare candidate proteins or material components and identify designs with greater mechanical robustness. The resulting force–extension profiles therefore connect molecular testing with the development of biomaterials and engineered proteins intended to withstand physical demands.
Single-molecule measurements establish how biomolecules respond when physical forces act on them. That molecular-scale information helps clarify how mechanical forces may regulate biological function across larger biological settings, including cells and tissues. In bioengineering, this connection supports interpretation of molecular stability and interactions in the context of broader mechanical behavior rather than as isolated molecular properties.