Abstract
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).
Original language | English (US) |
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Pages (from-to) | 8432-8435 |
Number of pages | 4 |
Journal | Angewandte Chemie - International Edition |
Volume | 50 |
Issue number | 36 |
DOIs | |
State | Published - Aug 29 2011 |
Keywords
- NMR spectroscopy
- bacteriorhodopsin
- membrane proteins
- protein structures
ASJC Scopus subject areas
- Catalysis
- Chemistry(all)