Backbone and methyl assignment of bacteriorhodopsin incorporated into nanodiscs.

ABSTRACT: Resonance assignments are challenging for membrane proteins due to the size of the lipid/detergent-protein complex and the presence of line-broadening from conformational exchange. As a consequence, many correlations are missing in the triple-resonance NMR experiments typically used for assignments. Herein, we present an approach in which correlations from these solution-state NMR experiments are supplemented by data from ¹³C unlabeling, single-amino acid type labeling, 4D NOESY data and proximity of moieties to lipids or water in combination with a structure of the protein. These additional data are used to edit the expected peaklists for the automated assignment protocol FLYA, a module of the program package CYANA. We demonstrate application of the protocol to the 262-residue

SUBMITTER: Kooijman L 

PROVIDER: S-EPMC7015963 | biostudies-literature | 2020 Jan

REPOSITORIES: biostudies-literature