Solid-state NMR (ssNMR) offers structural insight into the formation of molecular complexes for a wide range of molecular sizes and binding affinities (see, e.g.[1]). Recent instrumental and methodological progress has enabled novel possibilities for using multi-dimensional ssNMR to study molecular 3D structures and interactions in noncrystalline systems. In our group, such methods are used to study protein folding and aggregation on the atomic level and in a time-resolved manner for proteins involved in Alzheimer’s and Parkison’s disease (see, e.g.,[2]). In addition, we have developed a set of ssNMR experiments to study molecular structure, topology and complex formation in lipid bilayers. Such techniques can be used to characterize ligand binding to G-protein coupled receptors[3] or ion channels. For example, we have shown that high affinity toxin-binding to a chimeric Kv1.3 channel involves structural rearrangements of both constituents[4]. More recently, we have refined the ligand structure in the free and channel-bound state using ssNMR. Comparison to dynamical studies in solution suggests that an intrinsic structural plasticity underlies ion channel recognition. In addition to ligand-channel studies, ssNMR experiments are possible under variable physico-chemical conditions that may provide new insight into signal transduction in seven-helix receptors[5] and ion channel activation.
Life Sciences 2007 (2007) Proc Life Sciences, SA181
Research Symposium: Membrane protein complexes investigated by solid-state NMR
M. Baldus1, C. Ader1, G. Angerstein1, M. Engelhard3, M. Etzkorn1, I. de Gortari1, H. Heise1, O. Pongs2, R. Schneider1, K. Seidel1
1. MPI for Biophysical Chemistry, Gottingen, Germany. 2. Institut für Neurale Signalverarbeitung, Hamburg, Germany. 3. Max-Planck-Institut für molekulare Physiologie, Dortmund, Germany.
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