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NMR solution structure determination of membrane proteins reconstituted in detergent micelles
Author(s) -
Fernández César,
Wüthrich Kurt
Publication year - 2003
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(03)01155-4
Subject(s) - micelle , chemistry , membrane protein , nuclear magnetic resonance spectroscopy , membrane , peripheral membrane protein , integral membrane protein , protein–lipid interaction , lipid bilayer , crystallography , biochemistry , aqueous solution , organic chemistry
As an alternative to X‐ray crystallography, nuclear magnetic resonance (NMR) spectroscopy in solution can be used for three‐dimensional structure determination of small membrane proteins, preferably proteins with β‐barrel fold. This paper reviews recent achievements as well as limiting factors encountered in solution NMR studies of membrane proteins. Our particular interest has been focused on supplementing structure determination with data on the solvation of the proteins in the mixed micelles with detergents that are used to reconstitute membrane proteins for the NMR experiments. For the Escherichia coli outer membrane protein X (OmpX) in dihexanoylphosphatidylcholine (DHPC) micelles, such studies showed that the central part of the protein is covered with a fluid monolayer of lipid molecules, which seems to mimic quite faithfully the embedding of the protein in the lipid phase of the biological membrane. The implication is that the micellar systems used in this instance for the NMR studies of the membrane protein should also be suitable for further investigations of functional interactions with other proteins or low‐molecular weight ligands.