Magic-angle spinning NMR of intact bacteriophages: Insights into the capsid, DNA and their interface

Abramov, Gili; Morag, Omry; Goldbourt, Amir

doi:10.1016/j.jmr.2015.01.011

Cited by 18 publications

(14 citation statements)

References 103 publications

(131 reference statements)

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Virus capsids can also be studied by solid‐state NMR . NMR chemical shifts, and especially those of carbon‐13, are highly sensitive to backbone dihedral angles, and can detect conformational differences by chemical‐shift perturbations, typically when an interactant is added, or in protein complexes (for a review see Ref.…”

Section: Figurementioning

confidence: 99%

Localizing Conformational Hinges by NMR: Where Do Hepatitis B Virus Core Proteins Adapt for Capsid Assembly?

et al. 2018

View full text Add to dashboard Cite

The hepatitis B virus (HBV) icosahedral nucleocapsid is assembled from 240 chemically identical core protein molecules and, structurally, comprises four groups of symmetrically nonequivalent subunits. We show here that this asymmetry is reflected in solid-state NMR spectra of the capsids, in which peak splitting is observed for a subset of residues. We compare this information to dihedral angle variations from available 3D structures and also to computational predictions of "dynamic" domains and molecular hinges. We find that although, at the given resolution, dihedral angles variations directly obtained from the X-ray structures are not precise enough to be interpreted, the chemical-shift information from NMR correlates, and interestingly goes beyond, information from bioinformatics approaches. Our study reveals the high sensitivity with which NMR can detect the residues allowing the subtle conformational adaptations needed in lattice formation. Our findings are important for understanding the formation and modulation of protein assemblies in general.

show abstract

Section: Figurementioning

confidence: 99%

Localizing Conformational Hinges by NMR: Where Do Hepatitis B Virus Core Proteins Adapt for Capsid Assembly?

et al. 2018

View full text Add to dashboard Cite

show abstract

“…As ap roof of principle,weacquired 4D (H)COCANH, (H)CACONH, and (H)CBCANHs pectra of the 20 kDa bacteriophage tail-tube protein gp17.1 in at otal time of two and ah alf weeks.T hese spectra were sufficient to obtain complete resonance assignments in as traightforwardm anner without use of previous solution NMR data.Solid-state NMR is as pectroscopic technique that can be applied to investigate the structure and dynamics of insoluble proteins,i ncluding amyloid fibrils, [1,2] functional supramolecular assemblies, [3,4] and membrane-integrated proteins, [5] at atomic resolution. [6][7][8] In contrast to other methods,solid-state NMR does not require long-range order and can operate with proteins under in vivo conditions,f or instance membrane proteins can be studied in lipid bilayers [9,10] or in nanodiscs. [11] In contrast to solution NMR, solid-state NMR is not limited…”

mentioning

confidence: 99%

Bacteriophage Tail‐Tube Assembly Studied by Proton‐Detected 4D Solid‐State NMR

et al. 2017

View full text Add to dashboard Cite

Obtaining unambiguous resonance assignments remains a major bottleneck in solid‐state NMR studies of protein structure and dynamics. Particularly for supramolecular assemblies with large subunits (>150 residues), the analysis of crowded spectral data presents a challenge, even if three‐dimensional (3D) spectra are used. Here, we present a proton‐detected 4D solid‐state NMR assignment procedure that is tailored for large assemblies. The key to recording 4D spectra with three indirect carbon or nitrogen dimensions with their inherently large chemical shift dispersion lies in the use of sparse non‐uniform sampling (as low as 2 %). As a proof of principle, we acquired 4D (H)COCANH, (H)CACONH, and (H)CBCANH spectra of the 20 kDa bacteriophage tail‐tube protein gp17.1 in a total time of two and a half weeks. These spectra were sufficient to obtain complete resonance assignments in a straightforward manner without use of previous solution NMR data.

show abstract

“…[98][99][100][101][102][103][104] The physical condition of a sample is a key determinant for NMR resolution, with crystalline preparation usually yielding more resolved spectra [105]. However, the most interesting targets for solid state NMR are precisely those that are harder (or impossible) to obtain in crystalline form, such as membrane proteins, [5][6][7][106][107][108][109] protein assemblies [110][111][112][113][114], pathological aggregates [57][58][59][60] and fibrils [119][120][121][122][123]3,[124][125][126].…”

Section: Biomaterials From the Nmr Standpointmentioning

confidence: 99%