Question

What was found by comparing PrP^c and PrP^Sc proteins using MS and gas phase sequencing?

Answer 1

Comparing
`PrP^c` and
`PrP^(Sc)` using mass spectrometry reveals their structural and conformational differences, key to understanding prion disease mechanisms.

Step-by-step explanation:

Comparing
`PrP^c` (normal cellular prion protein) and
`PrP^(Sc)`(scrapie isoform of the prion protein) using mass spectrometry (MS) and gas phase sequencing can reveal differences in their structure and conformation, even though they share the same amino acid sequence. Techniques like nano-liquid chromatography tandem mass spectrometry (LC-MS/MS) allow for the meticulous analysis of proteins, identifying differences in folding, post-translational modifications, or aggregation states between
`PrP^c` and
`PrP^(Sc)`.

The process involves protein extraction, preparation for MS such as reduction, alkylation, and digestion with enzymes, followed by peptide analysis using LC-MS/MS. This is crucial in understanding prion diseases, as
`PrP^(Sc)` tends to have a higher propensity for aggregation than
`PrP^c`, leading to the characteristic amyloid plaques found in these diseases.