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

Habenstein, Birgit; Loquet, Antoine

doi:10.1016/j.bpc.2015.07.003

Cited by 25 publications

(28 citation statements)

References 245 publications

(407 reference statements)

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“…Interestingly, the 3D structure model construction of amyloid fibrils often requires hybrid approaches, which employ data acquired using other techniques, such as X-ray diffraction to determine the cross-beta signature, or scanning transmission electron microscopy (STEM), which give information about the mass-per-unit-lengths parameters [33,45,113,114]. From such analysis, a data set, comprising knowledge about the molecular atomic structure from SSNMR experiment and fibril morphology with STEM analysis, will be the basis for the complex model calculation and energy minimization processes.…”

Section: Restraint Detection and Identificationmentioning

confidence: 99%

“…Additionally, a certain level of structural heterogeneity on the mesoscopic level often encountered in amyloid fibrils has hampered the use of cryo-electron microscopy (cryo-EM) until recently [30,31]. Solid-state NMR (SSNMR) is a method of choice to achieve keen characterization of supramolecular assemblies in general [32][33][34][35][36][37][38], and more specifically of amyloid fibrillar assemblies at high resolution [39][40][41][42], as illustrated with the first structure determination of prion amyloid fibrils achieved in 2008 [43] by Meier and coworkers or with the discovery of the 3D fold of amyloid fibrils of α-synuclein [44] and Aβ [45][46][47][48][49], solved by SSNMR techniques. SSNMR capacity to probe the local order of "imperfect" inhomogeneous biological assemblies stands behind its power over amyloid fibrils [50].…”

Section: Introductionmentioning

confidence: 99%

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3D structure determination of amyloid fibrils using solid-state NMR spectroscopy

Loquet

Mammeri

Staněk

et al. 2018

Methods

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The amyloid fold is structurally characterized by a typical cross-β architecture, which is under debate to represent an energy-favourable folding state that many globular or natively unfolded proteins can adopt. Being initially solely associated with amyloid fibrils observed in the propagation of several neurodegenerative disorders, the discovery of non-pathological (or "functional") amyloids in many native biological processes has recently further intensified the general interest invested in those cross-β supramolecular assemblies. The insoluble and non-crystalline nature of amyloid fibrils and their usually inhomogeneous appearance on the mesoscopic level pose a challenge to biophysical techniques aiming at an atomic-level structural characterization. Solid-state NMR spectroscopy (SSNMR) has granted breakthroughs in structural investigations on amyloid fibrils ranging from the assessment of the impact of polymorphism in disease development to the 3D atomic structure determination of amyloid fibrils. First landmark studies towards the characterization of atomic structures and interactions involving functional amyloids have provided new impulses in the understanding of the role of the amyloid fold in native biological functions. Over the last decade many strategies have been developed in protein isotope labelling, NMR resonance assignment, distance restraint determination and 3D structure calculation of amyloid fibrils based on SSNMR approaches. We will here discuss the emerging concepts and state-of-the-art methods related to the assessment of amyloid structures and interactions involving amyloid entities by SSNMR.

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Section: Restraint Detection and Identificationmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

3D structure determination of amyloid fibrils using solid-state NMR spectroscopy

Loquet

Mammeri

Staněk

et al. 2018

Methods

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“…is the first-order quadrupolar interaction defined by (3) where and represents the second-order quadrupolar interaction defined by (4) The explicit expressions of under MAS are obtained by the usual transformation of the electric-field gradient (EFG) tensor from its principal axis system (PAS)…”

Section: Adiabatic Inversion Behavior Of a Half-integer Quadrupolar Smentioning

confidence: 99%

“…Cross-polarization magic-angle spinning (CPMAS) 1 is arguably the most important technique for the characterization of molecular-level structures and dynamics by solid-state NMR. [2][3][4][5][6][7] CPMAS relies on the Hartmann-Hahn (HH) condition 1,8 that arises when the radiofrequency (rf) field applied at the Larmor frequency of a spin-locked nuclide (usually 1 H), matches the rf field applied on either a spin-1/2 or a quadrupolar nuclide, whose sensitivity is to be increased. [9][10][11][12][13][14][15][16][17][18] Although conventional CPMAS involving continuous-wave spin-locking fields on both channels has been effective for carrying out solid-state NMR experiments under moderate MAS rates and magnetic field strengths, this classical approach faces limitations for acquiring NMR spectra that span large bandwidths.…”

Section: Introductionmentioning

confidence: 99%

Adiabatic sweep cross-polarization magic-angle-spinning NMR of half-integer quadrupolar spins

Kim

Schurko

et al. 2017

Journal of Magnetic Resonance

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The use of frequency-swept radiofrequency (rf) pulses for enhancing signals in the magic-angle spinning (MAS) spectra of half-integer quadrupolar nuclides was explored. The broadband adiabatic inversion cross-polarization magic-angle spinning (BRAIN-CPMAS) method, involving an adiabatic inversion pulse on the S-channel and a simultaneous rectangular spin-lock pulse on the I-channel (H), was applied to I(1/2)→S(3/2) systems. Optimal BRAIN-CPMAS matching conditions were found to involve low rf pulse strengths for both the I- and S-spin channels. At these low and easily attainable rf field strengths, level-crossing events among the energy levels |3/2〉,|1/2〉,|-1/2〉,|-3/2〉 that are known to complicate the CPMAS of quadrupolar nuclei, are mostly avoided. Zero- and double-quantum polarization transfer modes, akin to those we have observed for I(1/2)→S(1/2) polarization transfers, were evidenced by these analyses even in the presence of the quadrupolar interaction. H-Na and H-B BRAIN-CPMAS conditions were experimentally explored on model compounds by optimizing the width of the adiabatic sweep, as well as the rf pulse powers of the H andNa/B channels, for different MAS rates. The experimental data obtained on model compounds containing spin-3/2 nuclides, matched well predictions from numerical simulations and from an average Hamiltonian theory model. Extensions to half-integer spin nuclides with higher spins and potential applications of this BRAIN-CPMAS approach are discussed.

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“…Structural characterization of amyloids, which constitute the physical basis of many fungal prions, is a considerable challenge, and one faced by the amyloid field in general. The most adapted technique to gain access to high-resolution structures of amyloid assemblies is currently solid-state nuclear magnetic resonance (NMR) (107). Other approaches include X-ray diffraction techniques that so far can only inform on the overall fold or fold modification.…”

Section: Fungal Prion Structuresmentioning

confidence: 99%

Amyloid Prions in Fungi

2016

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Prions are infectious protein polymers that have been found to cause fatal diseases in mammals. Prions have also been identified in fungi (yeast and filamentous fungi), where they behave as cytoplasmic non-Mendelian genetic elements. Fungal prions correspond in most cases to fibrillary β-sheet-rich protein aggregates termed amyloids. Fungal prion models and, in particular, yeast prions were instrumental in the description of fundamental aspects of prion structure and propagation. These models established the "protein-only" nature of prions, the physical basis of strain variation, and the role of a variety of chaperones in prion propagation and amyloid aggregate handling. Yeast and fungal prions do not necessarily correspond to harmful entities but can have adaptive roles in these organisms.

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

Cited by 25 publications

References 245 publications

3D structure determination of amyloid fibrils using solid-state NMR spectroscopy

3D structure determination of amyloid fibrils using solid-state NMR spectroscopy

Adiabatic sweep cross-polarization magic-angle-spinning NMR of half-integer quadrupolar spins

Amyloid Prions in Fungi

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