In their leading processes (Fig. 2O , arrowheads). Surface labeling of unpermeabilized embryos with antinAPPL and subsequent permeabilization and staining for Go verified that Go colocalizes with cell-surface APPL in the EP cells (data not shown). To examine the relationship between APP and Go expression in developing mammalian neurons, embryonic rat hippocampal neurons were isolated and fixed aft
Nal peptide (SignalP 3.0), transmembrane domains (transmembrane helices by hidden Markov model), and PEXEL motif. The transcript levels of cognate genes were derived from the DeRisi and co-worker (15) transcriptome data, orthologs were from the Plasmodium database (16), and genome-wide polymorphism data were obtained from a study by Mu et al. (17). Protein function was assigned based on published
Nal peptide (SignalP 3.0), transmembrane domains (transmembrane helices by hidden Markov model), and PEXEL motif. The transcript levels of cognate genes were derived from the DeRisi and co-worker (15) transcriptome data, orthologs were from the Plasmodium database (16), and genome-wide polymorphism data were obtained from a study by Mu et al. (17). Protein function was assigned based on published
Biochemical ways. Mechanically, the penetration of the host's skin by the tick enables the delivery of B. burgdorferi deep into the dermis, near the blood vessels. Biochemically, tick salivary proteins help B. burgdorferi establish an infection by modulating host activities, such as coagulation, fibrinolysis and the immune response47. One of the mechanisms by which OspC enhances bacterial coloniza
Harvested and resuspended in a lysis buffer containing 0.4 M sucrose, 50 mM 3-(Nmorpholino) propanesulfonic acid, pH 7.0, 10 mM NaCl, 5 mM EDTA, and 0.5 mM PMSF. Cells were broken using a bead beater, and centrifuged with 5,000 g for 30 min at 4 to remove glass beads and insoluble cell debris. The membrane and the soluble fractions were separated as previously described with slight modifications
Harvested and resuspended in a lysis buffer containing 0.4 M sucrose, 50 mM 3-(Nmorpholino) propanesulfonic acid, pH 7.0, 10 mM NaCl, 5 mM EDTA, and 0.5 mM PMSF. Cells were broken using a bead beater, and centrifuged with 5,000 g for 30 min at 4 to remove glass beads and insoluble cell debris. The membrane and the soluble fractions were separated as previously described with slight modifications
An NMR spectroscopist, frequently raise the following question: the structure of a homologous protein has been resolved by X-raycrystallography, does this ease the resonance assignment of my protein? The answer is unfortunately negative. Numerous effects control the NMR chemical shifts and thus, even for a protein with a known structure, it is nearly impossible to predict them. In other terms, the
An NMR spectroscopist, frequently raise the following question: the structure of a homologous protein has been resolved by X-raycrystallography, does this ease the resonance assignment of my protein? The answer is unfortunately negative. Numerous effects control the NMR chemical shifts and thus, even for a protein with a known structure, it is nearly impossible to predict them. In other terms, the