Related Experiment Video
Updated: May 6, 2026

Analysis of Somatic Hypermutation in the JH4 intron of Germinal Center B cells from Mouse Peyer's Patches
Published on: April 20, 2021
Strongly Enhanced Lifetime of Higher-Order Bimerons and Antibimerons
Shiwei Zhu1,2, Moritz A Goerzen1, Changsheng Song2
1Université de Toulouse, CNRS, CEMES, 31055 Toulouse, France.
None:
Magnetic bimerons, similar to skyrmions, are topologically nontrivial spin textures characterized by topological charge Q. Most studies so far have focused on low-Q solitons (|Q| ≤ 1), such as skyrmions, bimerons, and vortices. Here, we present the first calculations of the lifetimes of ring-like high-Q bimerons and demonstrate that they are fundamentally more stable than high-Q skyrmions over a wide range of temperature. To obtain realistic results, our chosen system is an experimentally feasible van der Waals interface, Fe3GeTe2/Cr2Ge2Te6. We show that the lifetimes of high-Q (anti)bimerons can exceed the lifetimes of those with |Q| = 1 by 3 orders of magnitude. Remarkably, this trend remains valid even when extrapolated to room temperature (RT) because the lifetimes are dominated by entropy rather than energy barriers. This contrasts with high-Q skyrmions, whose lifetimes fall with |Q| near RT. We attribute this fundamental difference between skyrmions and bimerons to their distinct magnetic texture symmetries, which lead to different entropy-dominated lifetimes.
More Related Videos
13:14Generation of Discriminative Human Monoclonal Antibodies from Rare Antigen-specific B Cells Circulating in Blood
Published on: February 6, 2018
07:56Utilizing Time-Resolved Protein-Induced Fluorescence Enhancement to Identify Stable Local Conformations One α-Synuclein Monomer at a Time
Published on: May 30, 2021
Related Concept Videos
Immunological Memory
What is Immunological Memory?
Immunological memory is an integral function of the immune system that allows it to recognize and react more rapidly and effectively to pathogens previously encountered. This feature...
Antibody Structure and Classes
The basic structure of an antibody consists of four protein chains: two identical heavy chains and two identical light chains. These chains are held together by disulfide bonds and other non-covalent interactions, forming a Y-shaped structure.
Hybridoma Technology
Hybridoma Selection
Commonly used fusion techniques — electroporation,...
B Cell Activation and Differentiation
When naive B cells encounter a specific antigen that can bind to the B cell receptor (BCR) on their surface, they undergo sensitization to respond to the antigen's presence. Sensitization begins with...
Antibody Actions
Neutralization
Antibodies can bind to pathogens, preventing them from infecting host cells. This process...
Antibody Structure
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...