NMR Assignments for a Helical 40 kDa Membrane Protein
journal contributionposted on 28.04.2004 by Kirill Oxenoid, Hak Jun Kim, Jaison Jacob, Frank D. Sönnichsen, Charles R. Sanders
Any type of content formally published in an academic journal, usually following a peer-review process.
Backbone nuclear magnetic resonance (NMR) assignments were achieved for diacylglycerol kinase (DAGK) in detergent micelles. DAGK is a homotrimeric integral membrane protein comprised of 121 residue subunits, each having three transmembrane segments. Assignments were made using TROSY-based pulse sequences. DAGK was found to be an almost exclusively helical protein. This work points to the feasibility of both solving the structure of DAGK using solution NMR methods and using NMR as a primary tool in structural studies of other helical integral membrane proteins of similar size and complexity.