The "immunological synapse" is a membrane protein segregation structure that forms during contact between a lymphocyte and an antigen presenting cell (APC) during recognition of antigen by the lymphocyte.
In particular, hydrophobic matching of protein transmembrane segment length to lipid domains of similar thickness has been shown to affect membrane protein segregation, structure, and function [35], [36], [37], [38].
The formation of the protein segregation structure known as the "immunological synapse" in the contact region between B cells and antigen presenting cells appears to precede antigen (Ag) uptake by B cells.
A further 8 SNPs with biparental (AB × AB) segregation structures and 4 SNPs with AA × BB structures were identified.
The mesomorphic and microphase segregation structures of the block copolymers in bulk were studied by X-ray scattering, DSC and POM.
Figure 5 EDS patterns of the Ni element segregation structures.
Figure 4 EDS patterns of the Fe element segregation structures formed in the experiment.
SNPs in four R gene loci showed biparental segregation structures, mapping to the equivalent LG position in each parental map, and hence provide bridging markers.
In contrast to a differentiation of the ER into distinct subregions with different protein content, e.g. reticulons which accumulate at edges of ER sheets [ 27, 28], we observe a segregation of the DMP1-eGFP-labeled structures from the ER, resulting in two physically disconnected membrane networks.
A double-segregation-layer structure is also observed, with the coherent{10¯11}1} TB lying on one of these two layers.
Here we have overcome these limitations and developed an automated platform for high-content RNAi screening by time-lapse fluorescence microscopy of live HeLa cells expressing histone-GFP to report on chromosome segregation and structure.
