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Cross-linking strategies with proteins

Scheme 12 Strategy for phosphorylated protein/peptide recognition by chemosensors 37, 38 applying a cross-linking interaction with two phosphate groups on a protein surface... Scheme 12 Strategy for phosphorylated protein/peptide recognition by chemosensors 37, 38 applying a cross-linking interaction with two phosphate groups on a protein surface...
NA isolation and molecular characterization will be important to define the origin and functions of these proteins. At this time, infected cell nuclei offer the only source of these proteins, and NA have proved resistant to classic nuclear extraction methods (Yao and Jasmer, 1998). NA can be solubilized under conditions that co-extract nuclear lamins a/c and b (4 M urea, pH 8.0). Despite these similar physical properties, NA do not co-localize with lamins in the nucleoskeleton. However, both disulphide bonds and ionic interactions appear to contribute to nuclear complexes containing NA. In addition, NA can be cross-linked within host nuclei with protein cross-linking reagents. The foregoing properties represent current information available for the development of strategies to isolate and characterize these proteins and to investigate host proteins with which NA interact. [Pg.139]


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See also in sourсe #XX -- [ Pg.22 ]

See also in sourсe #XX -- [ Pg.22 ]




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