Ontology highlight
ABSTRACT:
SUBMITTER: Chang YC
PROVIDER: S-EPMC3890813 | biostudies-other | 2014 Jan
REPOSITORIES: biostudies-other
Chang Yu-Chu YC Bowie James U JU
Proceedings of the National Academy of Sciences of the United States of America 20131223 1
The thermodynamic stability of proteins is typically measured at high denaturant concentrations and then extrapolated back to zero denaturant conditions to obtain unfolding free energies under native conditions. For membrane proteins, the extrapolations are fraught with considerable uncertainty as the denaturants may have complex effects on the membrane or micellar structure. We therefore sought to measure stability under native conditions, using a method that does not perturb the properties of ...[more]