Structural and dynamic studies of proteins by high-resolution solid-state NMR

Böckmann, Anja

doi:10.1016/j.crci.2005.06.008

Cited by 25 publications

(23 citation statements)

References 106 publications

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“…2c) to measure and correlate the isotropic 13 C chemical shifts of dipoledipole-coupled 13 C-13 C spin pairs in different AGUs. PDSD is frequently used for studies of protein structure (Böckmann, 2006;Manolikas, Herrmann, & Meier, 2008) and is especially convenient to use for 13 C-13 C correlations, where MAS removes dipolar couplings between the 13 C spins. The addition of DARR, a weak RF-pulse during the mixing time ( mix ), further increases the recoupling of the dipolar interactions.…”

Section: Solid-state Nmr Spectroscopymentioning

confidence: 99%

13C NMR assignments of regenerated cellulose from solid-state 2D NMR spectroscopy

Idström

Schantz

Sundberg

et al. 2016

Carbohydrate Polymers

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From the assignment of the solid-state (13)C NMR signals in the C4 region, distinct types of crystalline cellulose, cellulose at crystalline surfaces, and disordered cellulose can be identified and quantified. For regenerated cellulose, complete (13)C assignments of the other carbon regions have not previously been attainable, due to signal overlap. In this study, two-dimensional (2D) NMR correlation methods were used to resolve and assign (13)C signals for all carbon atoms in regenerated cellulose. (13)C-enriched bacterial nanocellulose was biosynthesized, dissolved, and coagulated as highly crystalline cellulose II. Specifically, four distinct (13)C signals were observed corresponding to conformationally different anhydroglucose units: two signals assigned to crystalline moieties and two signals assigned to non-crystalline species. The C1, C4 and C6 regions for cellulose II were fully examined by global spectral deconvolution, which yielded qualitative trends of the relative populations of the different cellulose moieties, as a function of wetting and drying treatments.

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Section: Solid-state Nmr Spectroscopymentioning

confidence: 99%

13C NMR assignments of regenerated cellulose from solid-state 2D NMR spectroscopy

Idström

Schantz

Sundberg

et al. 2016

Carbohydrate Polymers

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“…While originally established on microcrystalline protein preparations,24–28 solid-state MAS NMR is becoming a more and more valuable approach for structural studies of biological solids that lack long-range order, such as macromolecular assemblies,29–31 disordered fibrils,32–35 membrane proteins,36–42 and biomaterials 43–45. Recent advances in multidimensional methods for resonance assignments and structural characterization by MAS NMR have made it possible to obtain detailed structural information on uniformly enriched proteins using only 0.1–0.5 μmoles of material 26–28,30,38,46–53…”

Section: Introductionmentioning

confidence: 99%

Solid-State NMR Studies of HIV-1 Capsid Protein Assemblies

Han

Ahn²,

Concel³

et al. 2010

J. Am. Chem. Soc.

109

153

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In mature HIV-1 virions, a 26.6 kDa CA protein is assembled into a characteristic cone shaped core (capsid) that encloses the RNA viral genome. The assembled capsid structure is best described by a fullerene cone model that is made up from a hexameric lattice containing a variable number of CA pentamers, thus allowing for closure of tubular or conical structures. In this report, we present a solid-state NMR analysis of the wild type HIV-1 CA protein, prepared as conical and spherical assemblies that are stable and are not affected by magic angle spinning of the samples at frequencies between 10 and 25 kHz. Multidimensional homo- and heteronuclear correlation spectra of CA assemblies of uniformly 13C,15N-labelled CA exhibit narrow lines, indicative of conformational homogeneity of the protein in these assemblies. For the conical assemblies, partial residue-specific resonance assignments were obtained. Analysis of the NMR spectra recorded for the conical and spherical assemblies indicates that the CA protein structure is not significantly different in the different morphologies. The present results demonstrate that the assemblies of CA protein are amenable to detailed structural analysis by solid-state NMR spectroscopy.

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“…Site-specific resonance assignment is therefore key to understanding phage properties. Many pulse sequences aimed at chemical shift assignments have been developed and are based on the acquisition of multi-dimensional experiments involving well established dipolar-based and J-based correlations of 1 H, 15 N and 13 C nuclei [33,[56][57][58][59]. 13 as well as sidechain assignment.…”

Section: Chemical Shift Assignmentmentioning

confidence: 99%