Thermal Aggregation
Thermal Aggregation - Related Videos
09:42
Analysis of Thermal Expansion via Dilatometry
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2023
Source: J. Jacob Chavez, Ryan T. Davis, and Taylor D. Sparks, Department of Materials Science and Engineering, The University of Utah, Salt Lake City, UT Thermal expansion is extremely important when considering which materials will be used in systems that experience fluctuations in temperature. A high or low thermal expansion in a material may or may not be desirable, depending on the application. For instance, in a common liquid thermometer, a material with a high thermal expansion would be...
10:08
Purification and Aggregation of the Amyloid Precursor Protein Intracellular Domain
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Cited by 1 •
2012
A method for large-scale purification of the APP intracellular domain (AICD) is described. We also describe methodology to induce in vitro AICD aggregation and visualization by atomic force microscopy. The methods described are useful for biochemical/structural characterization of the AICD and the effects of molecular chaperones on its aggregation.
10:10
Aggregates for Concrete and Asphaltic Mixes
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2023
Source: Roberto Leon, Department of Civil and Environmental Engineering, Virginia Tech, Blacksburg, VA Concrete and asphalt are by far the most common construction materials used today. Concrete is a composite material consisting of cement, water, air, coarse aggregate, and fine aggregates. Fine aggregates are typically sands and coarse aggregates are natural or crushed rocks. Chemical admixtures to modify certain specific properties are also commonly used (i.e., superplasticizers to make the...
10:32
Thermal Diffusivity and the Laser Flash Method
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2023
Source: Elise S.D. Buki, Danielle N. Beatty, and Taylor D. Sparks, Department of Materials Science and Engineering, The University of Utah, Salt Lake City, UT The laser flash method (LFA) is a technique used to measure thermal diffusivity, a material specific property. Thermal diffusivity (α) is the ratio of how much heat is conducted relative to how much heat is stored in a material. It is related to thermal conductivity (), how much heat is transferred through a material due to a temperature...
08:59
4D Imaging of Protein Aggregation in Live Cells
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Cited by 4 •
2013
Cellular viability depends on timely and efficient management of protein misfolding. Here we describe a method for visualizing the different potential fates of a misfolded protein: refolding, degradation, or sequestration in inclusions. We demonstrate the use of a folding sensor, Ubc9ts, for monitoring proteostasis and aggregation quality control in live cells using 4D microscopy.
FAQs
Heat promotes aggregation by disturbing the noncovalent interactions that help maintain a protein’s structure. As partial unfolding occurs, exposed hydrophobic regions can contact neighboring molecules. Those contacts drive assembly into soluble oligomers or, under other conditions, insoluble deposits. This mechanism links a temperature-induced structural change to altered molecular behavior and provides a basis for stability testing.
Exposed hydrophobic regions create interaction sites that were previously buried within the folded protein. When neighboring molecules encounter these regions, they can associate and form larger assemblies. The resulting products may remain soluble as oligomers or become insoluble deposits. Distinguishing these outcomes helps researchers relate molecular destabilization to changes in biological function, product stability, or tissue behavior.
The difference reflects distinct physical outcomes of the same heat-related destabilization process. Soluble oligomers remain dispersed in solution, whereas insoluble deposits form larger material that separates from the surrounding solution. Identifying which outcome occurs helps characterize how a protein responds to heating and can clarify whether aggregation is associated mainly with altered function, reduced product stability, or tissue-related effects.
Researchers examine how a protein responds as temperature rises and use the resulting aggregation measurements as evidence of structural stability. A stronger aggregation response indicates a condition that may destabilize the protein, while comparisons among conditions can identify more protective formulations or storage environments. These findings support stability assessment and can contribute to predictions of product shelf life.
These studies help identify conditions that promote or limit aggregation in biologic drugs. Researchers can evaluate candidate formulations or storage conditions by determining whether they preserve protein stability during temperature stress. The results support selection of more robust product conditions, help identify destabilizing environments, and provide evidence for estimating how long a biologic may retain acceptable stability.
Heat-driven aggregation provides an experimental way to investigate how destabilized proteins progress from partial unfolding to larger assemblies. Because the process can produce soluble oligomers or insoluble deposits, it offers a framework for examining molecular events associated with misfolding. In medicine, these observations can help connect altered protein structure with possible effects on tissue behavior and disease research.