Determining Protein 3D Structure by Magic Angle Spinning NMR

  • Ovidiu C. Andronesi
  • Henrike Heise
  • Marc Baldus

Solid-state NMR has long been utilized to study biomolecular structure and dynamics ranging from applications to protein complexes [1] and nucleotides [2] to membrane proteins [3–5] and protein fibrils [6]. In the case of macroscopically oriented membrane peptides, solid-state NMR furthermore has provided structural constraints to assemble three-dimensional (3D) membrane protein structures (see Ref. [7] for a recent review). Under magic angle spinning (MAS) [8], structural investigations were focused for a long time on the determination of local structural parameters. Recently, substantial progress has been made in NMR methodology, instrumentation, and sample preparation that now permits 3D molecular structure determination under MAS from one or a limited set of NMR samples. These approaches will be discussed in the context of this chapter. The interested reader is also referred to a series of recent review articles [9–11].

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Copyright information

© Springer 2008

Authors and Affiliations

  • Ovidiu C. Andronesi
    • 1
  • Henrike Heise
    • 1
  • Marc Baldus
    • 1
  1. 1.Department for NMR-Based Structural BiologyMax Planck Institute for Biophysical ChemistryGöttingenGermany

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