Ontology highlight
ABSTRACT:
SUBMITTER: Lawless MJ
PROVIDER: S-EPMC5985033 | biostudies-literature | 2018 Feb
REPOSITORIES: biostudies-literature
Lawless Matthew J MJ Pettersson John R JR Rule Gordon S GS Lanni Frederick F Saxena Sunil S
Biophysical journal 20180201 3
Nitroxide- and Cu<sup>2+</sup>-based electron spin resonance (ESR) are combined to provide insight into the conformational states of the functionally important α-helix of the human glutathione S-transferase A1. Distance measurements on various spin-labeled dimeric human glutathione S-transferase A1-1 all result in bimodal distance distributions, indicating that the C-terminus exists in two distinct conformations in solution, one of which closely matches that found in the crystal structure of the ...[more]