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Related Concept Videos

Protein Organization01:13

Protein Organization

Overview
Protein Organization01:24

Protein Organization

Proteins are polymers of amino acid residues. They are versatile and responsible for different cellular functions, including DNA replication, molecular transport, catalysis, and structural support. Proteins have a hierarchical structure comprising at least three levels of organization: primary, secondary, and tertiary structure. Some large proteins have a quaternary structure where individual protein subunits are linked together.
The primary structure of a protein is its amino acid sequence.
Protein Folding01:22

Protein Folding

Overview
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 and Protein Structure02:15

Protein and Protein Structure

Proteins are one of the most abundant organic molecules in living systems and have the most diverse range of functions of all macromolecules. Proteins may be structural, regulatory, contractile, or protective. They may serve in transport, storage, or membranes; or they may be toxins or enzymes. Their structures, like their functions, vary greatly. They are all, however, amino acid polymers arranged in a linear sequence.
A protein's shape is critical to its function. For example, an enzyme can...
Amyloid Fibrils03:03

Amyloid Fibrils

Amyloid fibrils are aggregates of misfolded proteins.  Under most circumstances, misfolded proteins are either refolded by chaperone proteins or degraded by the proteasome. However, in the case of a mutation or a disease, these proteins can accumulate to form large clusters and often further assemble to form elongated fibers, called fibrils. 
Amyloid deposits were observed as early as 1639 in the liver and the spleen.   In 1854, Rudolph Virchow performed iodine staining, normally used to...

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Related Experiment Video

Updated: Jun 8, 2026

Stress Distribution During Cold Compression of Rocks and Mineral Aggregates Using Synchrotron-based X-Ray Diffraction
10:36

Stress Distribution During Cold Compression of Rocks and Mineral Aggregates Using Synchrotron-based X-Ray Diffraction

Published on: May 20, 2018

Protein aggregate structure under high pressure.

Andrew J Jackson1, Duncan J McGillivray

  • 1NIST Center for Neutron Research, Gaithersburg, MD 20899, USA.

Chemical Communications (Cambridge, England)
|October 14, 2010
PubMed
Summary
This summary is machine-generated.

High pressure reveals the inner structure of casein protein micelles. These insights into protein aggregation and stability under pressure are crucial for food science applications.

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Last Updated: Jun 8, 2026

Stress Distribution During Cold Compression of Rocks and Mineral Aggregates Using Synchrotron-based X-Ray Diffraction
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Area of Science:

  • Food science and technology
  • Biophysics
  • Structural biology

Background:

  • Casein protein micelles are complex colloidal structures essential in dairy products.
  • Understanding their behavior under stress is vital for food processing and stability.

Purpose of the Study:

  • To investigate the structural changes of casein micelles under high hydrostatic pressure.
  • To elucidate the impact of pressure on protein aggregation and micelle stability.

Main Methods:

  • In situ structural measurements using (ultra-)small angle neutron scattering.
  • Application of high pressures up to 350 MPa to casein micelle solutions.

Main Results:

  • Demonstrated the feasibility of studying casein micelle structure under extreme pressure conditions.
  • Provided insights into pressure-induced alterations in protein structure and micelle aggregation.

Conclusions:

  • High pressure can be used as a tool to probe casein micelle structure and stability.
  • Findings contribute to a deeper understanding of protein-ligand interactions and colloidal stability in food systems.