Cystathionine beta-synthase mutants exhibit changes in protein unfolding: conformational analysis of misfolded variants in crude cell extracts

@inproceedings{Hnzda2011CystathionineBM,
  title={Cystathionine beta-synthase mutants exhibit changes in protein unfolding: conformational analysis of misfolded variants in crude cell extracts},
  author={Ale{\vs} Hn{\'i}zda and Vojtěch Jurga and Kateřina Rakov{\'a} and V. Kozich},
  booktitle={Journal of Inherited Metabolic Disease},
  year={2011}
}
Protein misfolding has been proposed to be a common pathogenic mechanism in many inborn errors of metabolism including cystathionine β-synthase (CBS) deficiency. In this work, we describe the structural properties of nine CBS mutants that represent a common molecular pathology in the CBS gene. Using thermolysin in two proteolytic techniques, we examined conformation of these mutants directly in crude cell extracts after expression in E. coli. Proteolysis with thermolysin under native conditions… CONTINUE READING