Keywords

protein homeostasis, proteomic, mass spectrometry, protein quality, protein misfolding, protein aggregation, protein folding stability, human serum, transthyretin, cardiac amyloidosis, serum albumin, rheumatoid arthritis, protein footprinting, transferrin

Data Set Description Summary

This data set includes the supplementary data for chpaters 3 and 4 in the dissertation Quantifying Protein Quality to Understand Protein Homeostasis. It includes various excel worksheets that were used to generate the data reported in the dissertation. We make this data available to the public so anyone who wants to reproduce the results has the resources and access to other perspectives that weren't discussed in depth in the dissertation. Chapter 3 used mass-spectrometry to quantify the surface accessibility differences in human serum albumin (HSA)between patients with and without rheumatoid arthritis (RA). We found certain residues are less reactive in the RA group, indicating a structural change in HSA. Such structural changes, possibly caused by ligand binding, stabilized HSA and explained the heat denature curve shift we observed. Chapter 4 introduced a novel assay, Iodination Protein Stability Assay (IPSA). IPSA is used to quantify protein quality by measuring protein folding stability. This is the first in situ study, to our best knowledge, that measure the protein folding stability of proteins from human serum. We confirmed that IPSA has the sensitivity to measure the differences in protein folding stability between transferrin’s different iron-binding states.