First, we characterized, for proteins with a given structure, how their functions were distributed across sequence space.
Using flow cytometry on a fluorescence-activated cell sorting Canto II (BD Biosciences), platelets and PMap were characterized for surface protein levels with fluorescently labeled antibodies against CD61, CD62P or activated GPIIb/IIIa (PAC-1mAb; BD Biosciences).
Folding intermediates have been detected and characterized for many proteins.
However, the activation mechanism of most cytokine receptors remains still unclear, and while agonism and antagonism have been described for ligand-mimetic peptides, there has been no report of inverse agonism that has been characterized for G protein-coupled receptors (GPCRs).
These cells have been well characterized for GPI-protein and PrPC exocytosis [47], [72] and do not possess caveolae, but form de novo caveolae upon cav-1 transfection [45].
A ceramic capillary module is described and characterized for continuous food protein proteolysis and defined systematic proteolysome mapping.
On the basis of the predictions from this algorithm, mutants were constructed and characterized for a model protein, thioredoxin.
Synechocystis PCC 6803 strains overexpressing pepc, gene encoding the carbon fixing enzyme phosphoenolpyruvate carboxylase (PEPc), were constructed and characterized for growth, PEPc protein content and in vitro PEPc activities.
