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Advances in mass spectrometry have enabled examination of rare and modified proteins; modified proteins are turning out to be not rare at all.
However, homogeneously modified proteins are not easily isolated from natural sources or prepared using modification enzymes.
Some predominately modified proteins are indicated by arrows.
However, modified proteins are not generally suitable for adjuvants, as they are difficult to standardize, store, and administer, and may be immunogenic.
Such modified proteins are degraded by cellular proteolysis, releasing not only modified peptides but also the modified amino acid, which is eventually excreted in the urine [ 6].
Because polyhistidine tags are often used for protein purification,[ 18] modified proteins are easy to access, which makes our method a universal technique for the investigation of almost any soluble protein.
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The preparation of posttranslationally modified proteins is required to investigate the function and structure of modified proteins.
The accumulation of the dually modified proteins is transient, and in activated T cells but not naïve T cells is significantly enhanced by co-receptor engagement.
After transfer onto nitrocellulose, modified proteins were revealed by anti-dinitrophenol antibodies.
As before, covalently modified proteins were conjugated to biotin-azide and affinity purified.
Even more challenging than the site-selective generation of singly modified proteins is the homogenous modification of a protein in multiple distinct positions with different probes.
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