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Interestingly, the surface protein model also shows conservation of an exposed N-terminal region between β-strands 2 and 3 of the major β-sheet that is extending the DSBH core indicating that these residues might be important for interaction with other proteins [see Additional file 5].
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Furthermore, surface expression of a model surface protein was monitored by an enzymatic whole-cell assay and flow cytometry.
Notably, the A. marginale surface protein 1a (MSP1a) is a model molecule for these studies because it serves as a marker for strain identity, is both an adhesin necessary for infection of cells and an immuno-reactive protein and is also an indicator of the evolution of strain diversity.
Our virtual ligand concept uses the PocketPicker [21], [22] algorithm to calculate a discrete representation of one or more potential ligand binding pockets on the surface of a 3D protein model.
These data indicate regulated apical basolateral cell surface protein distribution in cell models.
The revelation and putative functional assignment of two distinct sub-clusters on the surface of the protein models should enable rational site-directed mutagenesis, including homologous reverse-substitution experiments, to map surface binding patches onto these proteins.
In this paper, the interaction between a peptide adsorbed to a surface and another peptide adsorbed to an opposing surface is studied using the lattice protein model.
The shell coated the surface of the protein, modeling its rugosity, and increasing the size of the protein by the equivalent of a single layer of bound water.
Last, we demonstrated that a fluorescently labeled protein model drug can be delivered by surface loaded nanospheres.
Immune response against circumsporozoite protein (CSP) of Plasmodium berghei, a major surface protein on the sporozoite, confers protection in various murine malaria models.
Recently, Łuksza and Lässig (2014) constructed an explicit fitness model based on sequence data from the hemagglutinin (HA1) surface protein.
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