The Conformation of Bacteriorhodopsin Loops in Purple Membranes Resolved by Solid‐State MAS NMR Spectroscopy

Making complements: Solid-state MAS NMR spectra of bacteriorhodopsin in its native purple membrane environment can be used to complement crystallographic studies of the protein by validating and redefining the (possibly distorted) loop structures. Backbone dihedral angles were extracted from the chemical shifts and compared to the crystal structures. Where there are conformational differences, the dihedral angles were used to recalculate the loop structure (see picture). Detailed facts of importance to specialist readers are published as ”Supporting Information”. Such documents are peer-reviewed, but not copy-edited or typeset. They are made available as submitted by the authors. Please note: The publisher is not responsible for the content or functionality of any supporting information supplied by the authors. Any queries (other than missing content) should be directed to the corresponding author for the article.