Abstract
Techniques for atomic-resolution structural biology have evolved during the past several decades. Breakthroughs in instrumentation, sample preparation, and data analysis that occurred in the past decade have enabled characterization of viruses with an unprecedented level of detail. Here we review the recent advances in magic-angle spinning (MAS) nuclear magnetic resonance (NMR) spectroscopy for structural analysis of viruses and viral assemblies. MAS NMR is a powerful method that yields information on 3D structures and dynamics in a broad range of experimental conditions. After a brief introduction, we discuss recent structural and functional studies of several viruses investigated with atomic resolution at various levels of structural organization, from individual domains of a membrane protein reconstituted into lipid bilayers to virus-like particles and intact viruses. We present examples of the unique information revealed by MAS NMR about drug binding, conduction mechanisms, interactions with cellular host factors, and DNA packaging in biologically relevant environments that are inaccessible by other methods.
Highlights
The contemporary structural biology toolbox developed over the past three to four decades enables a wide variety of systems to be studied with varying degrees of spatial and temporal resolution
While solution nuclear magnetic resonance (NMR) experiments mostly correlate atoms connected by a covalent chemical bond, magicangle spinning (MAS) NMR relies on through-space, dipolar interactions
We highlight the role of MAS NMR in yielding information about 3D structure, functionally important dynamics, and mechanisms, as well as interactions with cofactors and single-stranded DNA packaging, inaccessible by other means
Summary
The contemporary structural biology toolbox developed over the past three to four decades enables a wide variety of systems to be studied with varying degrees of spatial and temporal resolution. Solution nuclear magnetic resonance (NMR) spectroscopy is commonly used for determination of 3D structures and dynamics of proteins and characterization of functional interactions with binding partners. Solution NMR is limited by size and solubility, precluding characterization of large and/or insoluble systems, such as biological assemblies and intact viruses. In contrast to solution state, where narrow spectral lines are attained because molecules naturally rotate, in the specimens where fast molecular rotations are absent (e.g., large assemblies or generally any immobilized systems), mechanical rotation of a NMR sample preparation b MAS NMR experiments
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