Structure Determination of Membrane Proteins by Nuclear Magnetic Resonance Spectroscopy

Opella, Stanley J.

doi:10.1146/annurev-anchem-062012-092631

Cited by 66 publications

(60 citation statements)

References 145 publications

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“…In addition, NMR spectroscopy can provide insight into time-dependent chemical phenomena, including reaction kinetics and dynamics in solution and the solid state at atomic resolution [33]. Although the cumulative molecular mass of a protein-detergent complex, the oligomerization state of the protein and a limited dispersion of an NMR spectrum may pose formidable hurdles for the structural study of membrane proteins by solution-state NMR, significant advances in sample preparation and experimental NMR methods have established NMR spectroscopy as a powerful method for studying membrane proteins both in the solution and in the solid state [34,35].…”

Section: Nmr Spectroscopy Of Membrane Proteinsmentioning

confidence: 99%

Structure of the mammalian TSPO/PBR protein

Jaremko

Jaipuria

et al. 2015

Biochemical Society Transactions

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The 3D structure of the 18-kDa transmembrane (TM) protein TSPO (translocator protein)/PBR (peripheral benzodiazepine receptor), which contains a binding site for benzodiazepines, is important to better understand its function and regulation by endogenous and synthetic ligands. We have recently determined the structure of mammalian TSPO/PBR in complex with the diagnostic ligand PK11195 [1-(2-chlorophenyl)-N-methyl-N-(1-methylpropyl)-3-isoquinolinecarboxamide; Science 343, 1363-1366], providing for the first time atomic-level insight into the conformation of this protein, which is up-regulated in various pathological conditions including Alzheimer's disease and Parkinson's disease. Here, we review the studies which have probed the structural properties of mammalian TSPO/PBR as well as the homologues bacterial tryptophan-rich sensory proteins (TspOs) over the years and provide detailed insight into the 3D structure of mouse TSPO (mTSPO)/PBR in complex with PK11195.

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Section: Nmr Spectroscopy Of Membrane Proteinsmentioning

confidence: 99%

Structure of the mammalian TSPO/PBR protein

Jaremko

Jaipuria

et al. 2015

Biochemical Society Transactions

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“…For detailed discussions of applications of SSNMR spectroscopy to biological systems, readers are referred to recently published comprehensive reviews. [1][2][3][4][5][6][7][8][9][10] …”

Section: Introductionmentioning

confidence: 99%

Recent Advances in Magic‐Angle Spinning Solid‐State NMR of Proteins

Ladizhansky¹

2014

Israel Journal of Chemistry

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Magic‐angle spinning (MAS) solid‐state NMR (SSNMR) spectroscopy is emerging as an important technique for the determination of three‐dimensional structures of biological molecules and for the characterization of their dynamics. While there is an established suite of MAS SSNMR experiments for protein structure determination in small‐ and medium‐sized proteins, these methods face many challenges in large systems. In this review, recent progress in MAS NMR spectroscopy is discussed, specifically focusing on the emerging developments aimed at improving the sensitivity and resolution of SSNMR that are likely to determine its future applications. These developments include sample preparation and isotopic labeling strategies, fast MAS, proton detection, and paramagnetic NMR spectroscopy.

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“…[1][2][3] This can be accomplished with protein-containing bilayer samples that are either magnetically or mechanically aligned relative to the magnetic field using Oriented Sample (OS) solid-state NMR or unoriented proteoliposomes samples using Rotationally Aligned (RA) solid-state NMR. 4 In the samples for both types of solidstate NMR experiments, the proteins undergo rapid rotational diffusion about the lipid bilayer normal.…”

Section: Introductionmentioning

confidence: 99%

Motion-adapted pulse sequences for oriented sample (OS) solid-state NMR of biopolymers

Opella

2013

The Journal of Chemical Physics

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One of the main applications of solid-state NMR is to study the structure and dynamics of biopolymers, such as membrane proteins, under physiological conditions where the polypeptides undergo global motions as they do in biological membranes. The effects of NMR radiofrequency irradiations on nuclear spins are strongly influenced by these motions. For example, we previously showed that the MSHOT-Pi4 pulse sequence yields spectra with resonance line widths about half of those observed using the conventional pulse sequence when applied to membrane proteins undergoing rapid uniaxial rotational diffusion in phospholipid bilayers. In contrast, the line widths were not changed in microcrystalline samples where the molecules did not undergo global motions. Here, we demonstrate experimentally and describe analytically how some Hamiltonian terms are susceptible to sample motions, and it is their removal through the critical π /2 Z-rotational symmetry that confers the "motion adapted" property to the MSHOT-Pi4 pulse sequence. This leads to the design of separated local field pulse sequence "Motion-adapted SAMPI4" and is generalized to an approach for the design of decoupling sequences whose performance is superior in the presence of molecular motions. It works by cancelling the spin interaction by explicitly averaging the reduced Wigner matrix to zero, rather than utilizing the 2π nutation to average spin interactions. This approach is applicable to both stationary and magic angle spinning solid-state NMR experiments. © 2013 AIP Publishing LLC.

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Structure Determination of Membrane Proteins by Nuclear Magnetic Resonance Spectroscopy

Cited by 66 publications

References 145 publications

Structure of the mammalian TSPO/PBR protein

Structure of the mammalian TSPO/PBR protein

Recent Advances in Magic‐Angle Spinning Solid‐State NMR of Proteins

Motion-adapted pulse sequences for oriented sample (OS) solid-state NMR of biopolymers

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