Solid-state NMR: An emerging technique in structural biology of self-assemblies

Biophys Chem. 2016 Mar;210:14-26. doi: 10.1016/j.bpc.2015.07.003. Epub 2015 Jul 16.

Abstract

Protein self-assemblies are ubiquitous biological systems involved in many cellular processes, ranging from bacterial and viral infection to the propagation of neurodegenerative disorders. Studying the atomic three-dimensional structures of protein self-assemblies is a particularly demanding task, as these systems are usually insoluble, non-crystalline and of large size. Solid-state NMR (ssNMR) is an emerging method that can provide atomic-level structural data on intact macromolecular assemblies. We here present recent progress in magic-angle spinning ssNMR to study protein assemblies and give an overview on its combination with complementary techniques such as cryo-EM, mass-per-length measurements, SAXS and X-ray diffraction. Applications of ssNMR on its own and in hybrid approaches have revealed precious atomic details and first high-resolution structures of complex biological assemblies, including amyloid fibrils, bacterial filaments, phages or virus capsids.

Keywords: Amyloid fibril; Bacterial filament; Hybrid structure determination; Protein supramolecular assembly; Solid-state NMR spectroscopy.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Crystallography, X-Ray
  • Magnetic Resonance Spectroscopy / methods*
  • Proteins / chemistry*

Substances

  • Proteins