By Hansen, Steen; Pedersen-Bjergaard, Stig
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Additional info for Bioanalysis of pharmaceuticals : sample preparation, separation techniques and mass spectrometry
The primary structure is the sequence of the covalently bonded amino acid chain. It is nothing more than a description of how the amino acids are arranged and which of the cysteine residues have formed disulfide bridges. The secondary structure is due to interactions between closely situated functional groups present in the side chains, and repeating structures occur. These structures are designated as ????-helixes, ????-sheets, and turns. The tertiary structure is caused by interactions between parts of the protein that are not situated closely together.
4 C C OH Free carboxy group at C-terminus O HN peptide peptide C NH2 Acetylation and amidation of terminal amino acids in a polypeptide chain Peptide Backbone Modifications Peptides and proteins can be modified at different stages. As early as in the production of biopharmaceuticals, modifications as a result of the (bio)synthesis process might occur. Also, after administration, the biopharmaceutical is prone to modification. All these modifications affect the sample preparation and analysis of the biomolecule.
The initial mobile phase when using gradient elution in this mode typically contains 90–95% organic solvent, and during the gradient an General Chromatographic Theory and Principles 45 increasing amount of water is added. It is therefore important to remember the rule that the sample should be dissolved in the mobile phase or something that is less strongly eluting. In this case, the organic solvent is the less strongly eluting solvent, whereas water is the stronger solvent. Injection of samples with a high content of water may therefore ruin the separation.