Abstract
Structural genomics of membrane proteins represents a particularly exciting challenge for biophysicists. These proteins are heterogeneous, both in themselves because of post translational modifications and in their environment from the heterogeneity of the membrane. Such heterogeneity greatly complicates structural characterization. Furthermore, the scarcity of specific interactions between secondary structural elements in the membrane environment results in increased dynamics and flexibility. Solid state NMR provides a methodology and a range of techniques that can characterize these proteins in a planar lipid bilayer environment [1]. NMR is an inherently high resolution method in that specific atomic sites are directly observed. With solid state NMR this potential for high resolution is fulfilled by obtaining very precise distance and orientational restraints. Until recently however, topology was very difficult to achieve; now several approaches are evolving so that both low resolution topology and unique high resolution structures can be obtained.
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Cross, T.A., Kim, S., Wang, J., Quine, J.R. (2001). From Topology to High Resolution Membrane Protein Structures. In: Kiihne, S.R., de Groot, H.J.M. (eds) Perspectives on Solid State NMR in Biology. Focus on Structural Biology, vol 1. Springer, Dordrecht. https://doi.org/10.1007/978-94-017-2579-8_6
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