Ontology highlight
ABSTRACT:
SUBMITTER: Dutta A
PROVIDER: S-EPMC4245987 | biostudies-literature | 2014 Nov
REPOSITORIES: biostudies-literature
Dutta Arpana A Altenbach Christian C Mangahas Sheryll S Yanamala Naveena N Gardner Eric E Hubbell Wayne L WL Klein-Seetharaman Judith J
Biochemistry 20141110 46
Rhodopsin is a model system for understanding membrane protein folding. Recently, conditions that allow maximally denaturing rhodopsin without causing aggregation have been determined, opening the door to the first structural characterization of denatured states of rhodopsin by nuclear magnetic resonance (NMR) and electron paramagnetic resonance (EPR) spectroscopy. One-dimensional 1H NMR spectra confirm a progressive increase in flexibility of resonances in rhodopsin with increasing denaturant c ...[more]