Protein structural dynamics by Magic-Angle Spinning NMR

Bonaccorsi, Marta; Marchand, Tanguy Le; Pintacuda, Guido

doi:10.1016/j.sbi.2021.02.008

Cited by 27 publications

(13 citation statements)

References 76 publications

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“…(a–c) Schematic representation of (b) spin relaxation caused by fluctuations of the anisotropic interactions and (c) direct measurement of scaled (motion-averaged) anisotropic interaction tensors, encoded in two chemical shift dimensions (a). Reproduced with permission from ref . Copyright 2021 Elsevier.…”

Section: H Detection and Protein Dynamicsmentioning

confidence: 99%

“…The top row shows the free form, whereas the bottom row shows the dorzolamide-bound form. Reprinted with permission from ref (copyright 2019 American Chemical Society) and from ref (copyright 2021 Elsevier).…”

Section: Structural and Dynamical Biology By 1h-detected Mas Nmrmentioning

confidence: 99%

“…Many reviews dealt with the topic of protein dynamics in the solid state. − In particular, Schanda and Ernst published a very elaborate topical review on all aspects of protein dynamics, and Rovó focused on relaxation–dispersion methods . Finally, our recent work highlights all recent developments in the field with a special focus on 1 H-detected methodological advances …”

Section: Introductionmentioning

confidence: 99%

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¹H-Detected Biomolecular NMR under Fast Magic-Angle Spinning

et al. 2022

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Since the first pioneering studies on small deuterated peptides dating more than 20 years ago, 1H detection has evolved into the most efficient approach for investigation of biomolecular structure, dynamics, and interactions by solid-state NMR. The development of faster and faster magic-angle spinning (MAS) rates (up to 150 kHz today) at ultrahigh magnetic fields has triggered a real revolution in the field. This new spinning regime reduces the 1H–1H dipolar couplings, so that a direct detection of 1H signals, for long impossible without proton dilution, has become possible at high resolution. The switch from the traditional MAS NMR approaches with 13C and 15N detection to 1H boosts the signal by more than an order of magnitude, accelerating the site-specific analysis and opening the way to more complex immobilized biological systems of higher molecular weight and available in limited amounts. This paper reviews the concepts underlying this recent leap forward in sensitivity and resolution, presents a detailed description of the experimental aspects of acquisition of multidimensional correlation spectra with fast MAS, and summarizes the most successful strategies for the assignment of the resonances and for the elucidation of protein structure and conformational dynamics. It finally outlines the many examples where 1H-detected MAS NMR has contributed to the detailed characterization of a variety of crystalline and noncrystalline biomolecular targets involved in biological processes ranging from catalysis through drug binding, viral infectivity, amyloid fibril formation, to transport across lipid membranes.

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Section: H Detection and Protein Dynamicsmentioning

confidence: 99%

Section: Structural and Dynamical Biology By 1h-detected Mas Nmrmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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¹H-Detected Biomolecular NMR under Fast Magic-Angle Spinning

et al. 2022

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“…In this study, we investigated CorA using two room-temperature methods, namely small-angle neutron scattering (SANS), sensitive to large amplitude conformational changes and magic-angle spinning solid-state NMR (MAS NMR), sensitive to structure and dynamics with atomic resolution ( Reif et al, 2021 ; Bonaccorsi et al, 2021 ). For both methods, we employ custom-developed state-of-the-art methodology, that is size-exclusion chromatography (SEC) coupled to SANS ( Johansen et al, 2018 ; Jordan et al, 2016 ) and match-out deuterated carrier systems for SANS ( Maric et al, 2014 ; Midtgaard et al, 2018 ) (so-called stealth carrier systems), and >100 kHz MAS NMR in lipid bilayers ( Schubeis et al, 2018 ; Schubeis et al, 2020 ).…”

Section: Introductionmentioning

confidence: 99%

Mg2+-dependent conformational equilibria in CorA and an integrated view on transport regulation

Johansen

Bonaccorsi

Bengtsen

et al. 2022

eLife

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The CorA family of proteins regulates the homeostasis of divalent metal ions in many bacteria, archaea, and eukaryotic mitochondria, making it an important target in the investigation of the mechanisms of transport and its functional regulation. Although numerous structures of open and closed channels are now available for the CorA family, the mechanism of the transport regulation remains elusive. Here, we investigated the conformational distribution and associated dynamic behaviour of the pentameric Mg2+ channel CorA at room temperature using small-angle neutron scattering (SANS) in combination with molecular dynamics (MD) simulations and solid-state nuclear magnetic resonance spectroscopy (NMR). We find that neither the Mg2+-bound closed structure nor the Mg2+-free open forms are sufficient to explain the average conformation of CorA. Our data support the presence of conformational equilibria between multiple states, and we further find a variation in the behaviour of the backbone dynamics with and without Mg2+. We propose that CorA must be in a dynamic equilibrium between different non-conducting states, both symmetric and asymmetric, regardless of bound Mg2+ but that conducting states become more populated in Mg2+-free conditions. These properties are regulated by backbone dynamics and are key to understanding the functional regulation of CorA.

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“…MAS NMR spectroscopy is a unique tool for investigation of structure and dynamic disorder of noncrystalline membrane protein complexes embedded in lipid bilayers (60)(61)(62). Here, we performed MAS NMR spectroscopy to address the structural dynamics of Zea-containing npq2 LHCII.…”

Section: Mas Nmr Spectroscopymentioning

confidence: 99%