| Protein Analysis - Characterizing Cancer-Fighting Lipopeptides | Sample Preparation |
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June 13, 2019 |
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The latest Protein Analysis news from across the AZoNetwork |
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 | | |  Stable Isotope-Labeled Protein Standards for Quantification Using MS
Mass spectrometry (MS) is considered the preferred technique for protein analysis in the field of proteomics. One strategy for accurate quantification is to spike in heavy isotope-labeled standards corresponding to the proteins of interest. QPrESTs are heavy isotope-labeled forms of the unlabeled (light) protein epitope signature tags or PrESTs utilized as antigens for producing antibodies. Their unique sequence design makes them perfect for MS-based quantification in complex samples.
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| | | | |  All proteins are made of basic secondary structure units, either α-helix or β-sheets, determined by hydrogen bonding between the amino acids within a peptide chain. On a larger scale, structures are formed by the combination of these secondary structures, and these can form supersecondary structures known as “motifs”. | | | | |  The biopharmaceutical industry develops drugs that are based on recombinant proteins expressed in different host systems, such as bacteria, yeast, fungi, plant cells, etc. In these cases, the expressed proteins are subjected to several rounds of purification to ensure that the host cell proteins do not contaminate the resulting proteins of interest. | | | | |  For most proteins that have had their structure determined, this has been done using protein crystallography. When the macromolecular structure of a protein is determined in this way, it is firstly crystalized by supersaturation, which causes each protein molecule to stack with its neighbors in a repeating pattern. The sample then undergoes x-ray crystallography, which is used to examine the structure of various crystal structures. | |
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