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Rabbit immunoglobulin G antigen (IgG) and carcinoembryonic antigen (CEA) were chosen as model proteins for analysis.
α-chymotrypsin and IgG were selected as model proteins for the clinically relevant neurotrophin-3 and anti-NogoA.
Finally, the on-line electrochemical tagging of cysteine residues was applied to the analysis of tryptic peptides of purified model proteins for protein identification through peptide mass fingerprinting.
The development of the water-soluble peptide self-assembly mimic (PSAM) system has provided a set of ideal model proteins for experimentally exploring the properties and minimal dye-binding requirements of amyloid fibrils.
For the purpose, binary proteins BSA and LYZ, which have different molecular weights and pI values, were used as model proteins for protein separation.
Two aggregation-prone monoclonal antibodies (mAb1 and mAb2) were used as model proteins for this study.
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Calmodulin was selected as a model protein for molecular assembly.
These characteristics make PhCutA1 a good model protein for investigating the role of charged residues in the stability of proteins from hyperthermophiles12,21,22,23,24.
Lactate dehydrogenase (LDH), a tetrameric protein, was selected as a model protein for this study.
Gelatin was employed as a model protein for matrix structure formation.
Bovine serum albumin (BSA) was used as a model protein for release studies.
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Justyna Jupowicz-Kozak
CEO of Professional Science Editing for Scientists @ prosciediting.com