Expanding the horizons for structural analysis of fully protonated protein assemblies by NMR spectroscopy at MAS frequencies above 100 kHz
| Autor: | Tatyana Polenova, Jodi Kraus, Jan Stanek, Werner E. Maas, Caitlin M. Quinn, Guangjin Hou, Loren B. Andreas, Anne Lesage, Jochem Struppe, Xingyu Lu, Angela M. Gronenborn, Manman Lu, Mingzhang Wang, Guido Pintacuda, Daniela Lalli |
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| Přispěvatelé: | Bruker BioSpin Corporation, University of Pittsburgh School of Medicine, Pennsylvania Commonwealth System of Higher Education (PCSHE), Department of Chemistry and Biochemistry, University of Delaware [Newark], Biological Solid-State NMR Methods - Méthodes de RMN à l'état solide en biologie, Institut des Sciences Analytiques (ISA), Institut de Chimie du CNRS (INC)-Université Claude Bernard Lyon 1 (UCBL), Université de Lyon-Université de Lyon-Centre National de la Recherche Scientifique (CNRS)-Institut de Chimie du CNRS (INC)-Université Claude Bernard Lyon 1 (UCBL), Université de Lyon-Université de Lyon-Centre National de la Recherche Scientifique (CNRS), Solid-State NMR Methods for Materials - Méthodes de RMN à l'état solide pour les matériaux, Department of Structural Biology, Pennsylvania Commonwealth System of Higher Education (PCSHE)-Pennsylvania Commonwealth System of Higher Education (PCSHE), This work was supported by the National Institutes of Health (NIH Grant P50 GM082251), we acknowledge the support of the National Science Foundation (NSF Grant CHE0959496) for the acquisition of the 850 MHz NMR spectrometer, and the National Institutes of Health (NIH Grant P30GM110758) for the support of core instrumentation infrastructure at the University of Delaware. |
| Jazyk: | angličtina |
| Rok vydání: | 2017 |
| Předmět: |
0301 basic medicine
Nuclear and High Energy Physics Proton Analytical chemistry Protonation 010402 general chemistry 01 natural sciences Article 03 medical and health sciences Nuclear magnetic resonance [CHIM.ANAL]Chemical Sciences/Analytical chemistry [SDV.BBM]Life Sciences [q-bio]/Biochemistry Molecular Biology Protein assemblies Instrumentation Nuclear Magnetic Resonance Biomolecular Radiation Chemistry Resolution (electron density) Resonance Proteins General Chemistry Nuclear magnetic resonance spectroscopy HIV-1 capsid protein 0104 chemical sciences Dipole 030104 developmental biology Heteronuclear molecule Proton-detected MAS NMR correlations HIV-1 MAS NMR Capsid Proteins Protons Two-dimensional nuclear magnetic resonance spectroscopy Oligopeptides |
| Zdroj: | Solid State Nuclear Magnetic Resonance Solid State Nuclear Magnetic Resonance, Elsevier, 2017, 87, pp.117-125. ⟨10.1016/j.ssnmr.2017.07.001⟩ |
| ISSN: | 0926-2040 |
| DOI: | 10.1016/j.ssnmr.2017.07.001⟩ |
| Popis: | International audience; The recent breakthroughs in NMR probe technologies resulted in the development of MAS NMR probes with rotation frequencies exceeding 100 kHz. Herein, we explore dramatic increases in sensitivity and resolution observed at MAS frequencies of 110-111 kHz in a novel 0.7 mm HCND probe that enable structural analysis of fully protonated biological systems. Proton- detected 2D and 3D correlation spectroscopy under such conditions requires only 0.1-0.5 mg of sample and a fraction of time compared to conventional 13C-detected experiments. We discuss the performance of several proton- and heteronuclear- (13C-,15N-) based correlation experiments in terms of sensitivity and resolution, using a model microcrystalline fMLF tripeptide. We demonstrate the applications of ultrafast MAS to a large, fully protonated protein assembly of the 231-residue HIV-1 CA capsid protein. Resonance assignments of protons and heteronuclei, as well as 1H-15N dipolar and 1HN CSA tensors are readily obtained from the high sensitivity and resolution proton-detected 3D experiments. The approach demonstrated here is expected to enable the determination of atomic-resolution structures of large protein assemblies, inaccessible by current methodologies. |
| Databáze: | OpenAIRE |
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