Folding of G_α Subunits: Implications for Disease States.

ABSTRACT: G-proteins play a central role in signal transduction by fluctuating between "on" and "off" phases that are determined by a conformational change. cAMP is a secondary messenger whose formation is inhibited or stimulated by activated G_iα1 or G_sα subunit. We used tryptophan fluorescence, UV/vis spectrophotometry, and circular dichroism to probe distinct structural features within active and inactive conformations from wild-type and tryptophan mutants of G_iα1 and G_sα. For all proteins studied, we found that the active conformations were more stable than the inactive conformations, and upon refolding from higher temperatures, activated wild-type subunits recovered significantly more native structure. We also observed that the wild-type subunits parti

SUBMITTER: Najor M 

PROVIDER: S-EPMC6210069 | biostudies-literature | 2018 Oct

REPOSITORIES: biostudies-literature