scholarly journals Biologische Festkörper-NMR-Spektroskopie in der Strukturbiologie

BIOspektrum ◽  
2021 ◽  
Vol 27 (3) ◽  
pp. 257-259
Author(s):  
Nils-Alexander Lakomek
Keyword(s):  
Solid State Nmr ◽  
Structural Information ◽  
Magic Angle Spinning ◽  
Magic Angle ◽  
Structure And Dynamics ◽  
Wide Range ◽  
Recent Developments ◽  
Lipid Environment ◽  
Angle Spinning ◽  
Fast Magic Angle Spinning

AbstractBiological solid-state NMR elucidates the structure and dynamics of biomolecules at physiological temperatures. It provides high-resolution structural information for a wide range of biomolecules and assemblies, from small membrane proteins embedded in a lipid environment, over fibrillar structures up to supramolecular assemblies. Recent developments allow for proton detection at fast magic angle spinning frequencies, which reduces the required sample amounts to a few hundreds of micrograms.

scholarly journals Frequency-selective Heteronuclear Correlation (FS-HETCOR) Experiments in Solid-State NMR

2021 ◽  
Author(s):  
Zhengfeng Zhang ◽  
Yongchao Su ◽  
Jun Yang
Keyword(s):  
Solid State ◽  
Solid State Nmr ◽  
Structural Information ◽  
Magic Angle Spinning ◽  
Magic Angle ◽  
Heteronuclear Correlation ◽  
Selective Pulses ◽  
Frequency Selective ◽  
Angle Spinning ◽  
Fast Magic Angle Spinning

Heteronuclear correlation (HETCOR) is critical to obtain structural information in solid-state nuclear magnetic resonance (NMR). We propose novel frequency-selective Heteronuclear correlation (FS-HETCOR) experiments to selectively enhance the inter-atomic correlations of interest. FS-HETCOR relies on heteronuclear selective phase-optimized recoupling (SPRx), which is frequency-selective in heteronuclear recouping without using selective pulses. Compared to regular HETCOR, FS-HETCOR selectively enhances the desired heteronuclear correlations by a factor of up to 5 and suppresses the unwanted ones to 10% as demonstrated in 1H-19F and 1H-13C experiments under fast magic-angle spinning (MAS). Moreover, FS-HETCOR can theoretically be applied at arbitrary MAS rates by utilizing various SPRx schemes. We believe that the method will enhance the ability of solid-state NMR to probe heteronuclear structural information.

scholarly journals Residue-specific insights into (2x)72 kDa tryptophan synthase obtained from fast-MAS 1H-detected solid-state NMR

2021 ◽  
Author(s):  
Alexander Klein ◽  
Petra Rov&oacute ◽  
Varun V. Sakhrani ◽  
Yangyang Wang ◽  
Jacob Holmes ◽  
...  
Keyword(s):  
Solid State ◽  
Solid State Nmr ◽  
Chemical Properties ◽  
Magic Angle Spinning ◽  
Precise Determination ◽  
Magic Angle ◽  
Tryptophan Synthase ◽  
Recent Developments ◽  
Angle Spinning ◽  
Fast Magic Angle Spinning

Solid-state NMR has emerged as a potent technique in structural biology, suitable for the study of fibrillar, micro-crystalline, and membrane proteins. Recent developments in fast-magic-angle-spinning and proton-detected methods have enabled detailed insights into structure and dynamics, but molecular-weight limitations for the asymmetric part of target proteins have remained at ~30-40 kDa. Here we employ solid-state NMR for atom-specific characterization of the 72 kDa (asymmetric unit) microcrystalline protein tryptophan synthase, an important target in pharmacology and biotechnology, chemical-shift assignments of which we obtain via higher-dimensionality, 4D and 5D solid-state NMR experiments. The assignments for the first time provide comprehensive data for assessment of side chain chemical properties involved in the catalytic turnover, and, in conjunction with first-principles calculations, precise determination of thermodynamic and kinetic parameters is demonstrated for the essential acid-base catalytic residue βK87. The insights provided by this study expand by nearly a factor of two the size limitations widely accepted for NMR today, demonstrating the applicability of solid-state NMR to systems that have been thought to be out of reach due to their complexity.

scholarly journals Exact distance measurements for structure and dynamics in solid proteins by fast-magic-angle-spinning NMR

2019 ◽  
Vol 55 (55) ◽  
pp. 7899-7902 ◽  
Author(s):  
Kristof Grohe ◽  
Evgeny Nimerovsky ◽  
Himanshu Singh ◽  
Suresh K. Vasa ◽  
Benedikt Söldner ◽  
...  
Keyword(s):  
Solid State ◽  
Solid State Nmr ◽  
Protein Structures ◽  
Magic Angle Spinning ◽  
Magic Angle ◽  
Distance Measurements ◽  
Structure And Dynamics ◽  
Distance Restraints ◽  
Angle Spinning ◽  
Fast Magic Angle Spinning

With the integrative “eRFDR” approach, turning qualitative into exact distance restraints, high-resolution protein structures are obtained by fast-magic-angle-spinning solid-state NMR.

scholarly journals Recent developments in solid–state magic–angle spinning, nuclear magnetic resonance of fully and significantly isotopically labelled peptides and proteins

2004 ◽  
Vol 359 (1446) ◽  
pp. 997-1008 ◽  
Author(s):  
Suzana K. Straus
Keyword(s):  
Nuclear Magnetic Resonance ◽  
Solid State ◽  
Magnetic Resonance ◽  
Solid State Nmr ◽  
Structural Information ◽  
Magic Angle Spinning ◽  
Magic Angle ◽  
Recent Developments ◽  
Angle Spinning ◽  
Nuclear Magnetic

In recent years, a large number of solid–state nuclear magnetic resonance (NMR) techniques have been developed and applied to the study of fully or significantly isotopically labelled ( 13 C, 15 N or 13 C/ 15 N) biomolecules. In the past few years, the first structures of 13 C/ 15 N–labelled peptides, Gly–Ile and Met–Leu–Phe, and a protein, Src–homology 3 domain, were solved using magic–angle spinning NMR, without recourse to any structural information obtained from other methods. This progress has been made possible by the development of NMR experiments to assign solid–state spectra and experiments to extract distance and orientational information. Another key aspect to the success of solid–state NMR is the advances made in sample preparation. These improvements will be reviewed in this contribution. Future prospects for the application of solid–state NMR to interesting biological questions will also briefly be discussed.

Characterization of Polymer Compatibility by1H Dipolar Filter Solid-State NMR under Fast Magic Angle Spinning

2007 ◽  
Vol 40 (25) ◽  
pp. 9018-9025 ◽  
Author(s):  
Xiaoliang Wang ◽  
Qiang Gu ◽  
Qing Sun ◽  
Dongshan Zhou ◽  
Pingchuan Sun ◽  
...  
Keyword(s):  
Solid State ◽  
Solid State Nmr ◽  
Magic Angle Spinning ◽  
Magic Angle ◽  
Polymer Compatibility ◽  
Angle Spinning ◽  
Fast Magic Angle Spinning

Very fast magic angle spinning 1H-14N 2D solid-state NMR: Sub-micro-liter sample data collection in a few minutes

2011 ◽  
Vol 208 (1) ◽  
pp. 44-48 ◽  
Author(s):  
Yusuke Nishiyama ◽  
Yuki Endo ◽  
Takahiro Nemoto ◽  
Hiroaki Utsumi ◽  
Kazuo Yamauchi ◽  
...  
Keyword(s):  
Solid State ◽  
Data Collection ◽  
Solid State Nmr ◽  
Magic Angle Spinning ◽  
Magic Angle ◽  
Sample Data ◽  
Angle Spinning ◽  
Fast Magic Angle Spinning

scholarly journals Dihedral Angle Measurements for Structure Determination by Biomolecular Solid-State NMR Spectroscopy

2021 ◽  
Vol 8 ◽  
Author(s):  
Patrick C. A. van der Wel
Keyword(s):  
Solid State ◽  
Structure Determination ◽  
Solid State Nmr ◽  
Structural Information ◽  
Magic Angle Spinning ◽  
Magic Angle ◽  
Distance Measurements ◽  
Challenges And Opportunities ◽  
Molecule Interactions ◽  
Angle Spinning

In structural studies of immobilized, aggregated and self-assembled biomolecules, solid-state NMR (ssNMR) spectroscopy can provide valuable high-resolution structural information. Among the structural restraints provided by magic angle spinning (MAS) ssNMR the canonical focus is on inter-atomic distance measurements. In the current review, we examine the utility of ssNMR measurements of angular constraints, as a complement to distance-based structure determination. The focus is on direct measurements of angular restraints via the judicious recoupling of multiple anisotropic ssNMR parameters, such as dipolar couplings and chemical shift anisotropies. Recent applications are highlighted, with a focus on studies of nanocrystalline polypeptides, aggregated peptides and proteins, receptor-substrate interactions, and small molecule interactions with amyloid protein fibrils. The review also examines considerations of when and where ssNMR torsion angle experiments are (most) effective, and discusses challenges and opportunities for future applications.

Sign in / Sign up

Export Citation Format

Share Document