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Related Concept Videos

Antibody Structure01:10

Antibody Structure

Overview
Antibodies, also known as immunoglobulins (Ig), are essential players of the adaptive immune system. These antigen-binding proteins are produced by B cells and make up 20 percent of the total blood plasma by weight. In mammals, antibodies fall into five different classes, which each elicits a different biological response upon antigen binding.
The Y-Shaped Structure of Antibodies Consists of Four Polypeptide Chains
Antibodies consist of four polypeptide chains: two identical heavy...
Antibody Structure01:10

Antibody Structure

Overview
Antibodies, also known as immunoglobulins (Ig), are essential players of the adaptive immune system. These antigen-binding proteins are produced by B cells and make up 20 percent of the total blood plasma by weight. In mammals, antibodies fall into five different classes, which each elicits a different biological response upon antigen binding.
The Y-Shaped Structure of Antibodies Consists of Four Polypeptide Chains
Antibodies consist of four polypeptide chains: two identical heavy...
Western Blotting01:15

Western Blotting

Western blotting is an analytical technique for protein identification. It has various applications in immunology and medicine, including detecting diseases like bovine spongiform encephalopathy, mad cow disease, and human and feline immunodeficiency virus from biological samples.
The technique begins with separating proteins from the sample using sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE), followed by protein transfer, immunoblotting, and finally, protein detection.
Diversity of Antigen Receptors01:28

Diversity of Antigen Receptors

Antigen receptors are essential components of the immune system crucial in defending the body against foreign invaders. These receptors are present on the surface of B and T cells, enabling them to recognize antigens and mount an appropriate immune response.
Before encountering any antigen, lymphocytes express these receptors. On B cells, the antigen receptor is a membrane-bound antibody molecule called BCR; on T cells, it is a T cell receptor or TCR. B and T cell receptors are composed of two...

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Single-Molecule Localization Microscopy of Membrane Proteins using Single-Antibody Labeling
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Colorful horizons with charge in anti-de Sitter space.

Steven S Gubser1

  • 1Joseph Henry Laboratories, Princeton University, Princeton, New Jersey 08544, USA.

Physical Review Letters
|December 31, 2008
PubMed
Summary

Spontaneous symmetry breaking near black hole horizons is possible using non-Abelian gauge fields. This leads to a second-order phase transition in anti-de Sitter space.

Area of Science:

  • Theoretical Physics
  • Quantum Field Theory
  • General Relativity

Background:

  • Black hole thermodynamics and properties are crucial in understanding gravity.
  • Gauge symmetries play a fundamental role in particle physics and cosmology.
  • Anti-de Sitter space provides a theoretical framework for studying quantum gravity.

Purpose of the Study:

  • To investigate the possibility of spontaneous Abelian gauge symmetry breaking near black hole horizons.
  • To explore the role of non-Abelian gauge fields in this process.
  • To characterize the phase transitions associated with symmetry breaking.

Main Methods:

  • Utilizing a condensate of non-Abelian gauge fields.
  • Analyzing Reissner-Nordström-anti-de Sitter black hole solutions.

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  • Investigating second-order phase transitions.

    • Main Results:

    • Demonstrated spontaneous breaking of Abelian gauge symmetry near the black hole horizon.
    • Identified a second-order phase transition.
    • Symmetry-breaking solutions preserve a specific combination of gauge and rotational invariance.

    Conclusions:

    • Spontaneous symmetry breaking is a viable mechanism near black hole horizons in anti-de Sitter space.
    • The identified phase transition offers new insights into black hole physics.
    • The preserved symmetries provide constraints for further theoretical development.