@article{TEXTUAL,
      recid = {5913},
      author = {Tian, Yu and Tirrell, Matthew and Davis, Carley and  Wesson, Jeffrey A.},
      title = {Protein primary structure correlates with calcium oxalate  stone matrix preference},
      journal = {PLOS ONE},
      address = {2021-09-23},
      number = {TEXTUAL},
      abstract = {<p>Despite the apparent importance of matrix proteins in  calcium oxalate kidney stone formation, the complexity of  the protein mixture continues to elude explanation. Based  on a series of experiments, we have proposed a model where  protein aggregates formed from a mixture containing both  strongly charged polyanions and strongly charged  polycations could initiate calcium oxalate crystal  formation and crystal aggregation to create a stone. These  protein aggregates also preferentially adsorb many weakly  charged proteins from the urine to create a complex protein  mixture that mimics the protein distributions observed in  patient samples. To verify essential details of this model  and identify an explanation for phase selectivity observed  in weakly charged proteins, we have examined primary  structures of major proteins preferring either the matrix  phase or the urine phase for their contents of aspartate,  glutamate, lysine and arginine; amino acids that would  represent fixed charges at normal urine pH of 6–7. We  verified enrichment in stone matrix of proteins with a  large number of charged residues exhibiting extreme  isoelectric points, both low (pI<5) and high (pI>9). We  found that the many proteins with intermediate isoelectric  points exhibiting preference for stone matrix contained a  smaller number of charge residues, though still more total  charges than the intermediate isoelectric point proteins  preferring the urine phase. While other sources of charge  have yet to be considered, protein preference for stone  matrix appears to correlate with high total charge  content.</p>},
      url = {http://knowledge.uchicago.edu/record/5913},
}