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1. Dynamic Nuclear Polarization-Enhanced Biomolecular NMR Spectroscopy at High Magnetic Field with Fast Magic-Angle Spinning

Author

Olivier Ouari, Diane Cala de Paepe, Inara Akopjana, Svetlana Kotelovica, G. Pintacuda, Anne Lesage, Andrea Pica, Andrew J. Pell, Kristaps Jaudzems, Andrea Bertarello, Sachin Rama Chaudhari, Emeline Barbet-Massin, Kaspars Tars, David Gajan, 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, Dipartimento di Scienze Chimiche, Università degli studi di Napoli Federico II, Department of Materials and Environmental Chemistry - Arrhenius Laboratory, Biomed Res & Study Ctr, Institut de Chimie Radicalaire (ICR), Aix Marseille Université (AMU)-Institut de Chimie du CNRS (INC)-Centre National de la Recherche Scientifique (CNRS), We acknowledge financial support from the CNRS, the EQUIPEX (contract ANR-10-EQPX-47-01), the Agence Nationale de la Recherche (contract ANR15-CE29-002202), and the People Programme of the European Union's FP7 (FP7- PEOPLE-2012-ITN no. 317127 'pNMR'). K.J. is supported by a MC incoming fellowship (REA grant agreement no. 661175 'virus-DNP-NMR'). A.P. is supported by Fondazione con il Sud (grant 2011-PDR-19)., ANR-10-EQPX-0047,SENS,RMN de Surface Exalté par Polarisation Dynamique Nucléaire(2010), European Project: 317127,EC:FP7:PEOPLE,FP7-PEOPLE-2012-ITN,PNMR(2013), Université Claude Bernard Lyon 1 (UCBL), Université de Lyon-Université de Lyon-Institut de Chimie du CNRS (INC)-Centre National de la Recherche Scientifique (CNRS)-Université Claude Bernard Lyon 1 (UCBL), Université de Lyon-Université de Lyon-Institut de Chimie du CNRS (INC)-Centre National de la Recherche Scientifique (CNRS), and University of Naples Federico II = Università degli studi di Napoli Federico II

Subjects
Materials science, magic-angle spinning, 010405 organic chemistry, General Medicine, General Chemistry, Nuclear magnetic resonance spectroscopy, 010402 general chemistry, Polarization (waves), 01 natural sciences, Molecular physics, Catalysis, Spectral line, 0104 chemical sciences, NMR spectra database, dynamic nuclear polarization, Paramagnetism, Magic angle spinning, [CHIM]Chemical Sciences, biomolecular NMR, solid-state NMR spectroscopy, High magnetic field, Coherence (physics)
Abstract

International audience; Dynamic nuclear polarization (DNP) is a powerful way to overcome the sensitivity limitation of magic-angle-spinning (MAS) NMR experiments. However, the resolution of the DNPNMR spectra of proteins is compromised by severe line broadening associated with the necessity to perform experiments at cryogenic temperatures and in the presence of paramagnetic radicals. High-quality DNP-enhanced NMR spectra of the Acinetobacter phage 205 (AP205) nucleocapsid can be obtained by combining high magnetic field (800MHz) and fast MAS (40kHz). These conditions yield enhanced resolution and long coherence lifetimes allowing the acquisition of resolved 2D correlation spectra and of previously unfeasible scalar-based experiments. This enables the assignment of aromatic resonances of the AP205 coat protein and its packaged RNA, as well as the detection of long-range contacts, which are not observed at room temperature, opening new possibilities for structure determination.

Published
2018
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2. Backbone and side-chain proton NMR assignment in fully protonated proteins: microcrystals, sedimented assemblies, and amyloid fibrils

Author

Stanek, Jan, Andreas, Loren, Jaudzems, Kristaps, Cala, Diane, Lalli, Daniela, Bertarello, Andrea, Schubeis, Tobias, Akopjana, Inara, Kotelovica, Svetlana, Tars, Kaspars, Pica, Andrea, Leone, Serena, Picone, Delia, Xu, Zhi-Qiang, Dixon, Nicholas, Martinez, Denis, Berbon, Melanie, El Mammeri, Nadia, Noubhani, Abdelmajid, Saupe, Sven, Habenstein, Birgit, Loquet, Antoine, Pintacuda, Guido, Biological Solid-State NMR Methods - Méthodes de RMN à l'état solide en biologie, Institut des Sciences Analytiques (ISA), Université Claude Bernard Lyon 1 (UCBL), Université de Lyon-Université de Lyon-Institut de Chimie du CNRS (INC)-Centre National de la Recherche Scientifique (CNRS)-Université Claude Bernard Lyon 1 (UCBL), Université de Lyon-Université de Lyon-Institut de Chimie du CNRS (INC)-Centre National de la Recherche Scientifique (CNRS), Biomed Res & Study Ctr, Latvian Biomed Res & Study Ctr, Dept Mol Biol, University of Latvia (LU), Dipartimento di Scienze Chimiche, University of Naples Federico II = Università degli studi di Napoli Federico II, School of Chemistry [Wollongong], University of Wollongong [Australia], Chimie et Biologie des Membranes et des Nanoobjets (CBMN), Université de Bordeaux (UB)-École Nationale d'Ingénieurs des Travaux Agricoles - Bordeaux (ENITAB)-Institut de Chimie du CNRS (INC)-Centre National de la Recherche Scientifique (CNRS), Institut de biochimie et génétique cellulaires (IBGC), Université Bordeaux Segalen - Bordeaux 2-Centre National de la Recherche Scientifique (CNRS), Fondation pour la Chimie des Substances Naturelles, IR-RMN FR3050, Fondazione con il Sud (grant 2011- PDR-19), European Project: 648974,H2020,ERC-2014-CoG,P-MEM-NMR(2015), European Project: 639020,H2020,ERC-2014-STG,Weakinteract(2015), European Project: 624918,EC:FP7:PEOPLE,FP7-PEOPLE-2013-IIF,MEM-MAS(2014), European Project: 661799,H2020,H2020-MSCA-IF-2014,COMPLEX-fastMAS-NMR(2016), European Project: 661175,H2020,H2020-MSCA-IF-2014,virus-DNP-NMR(2015), European Project: 317127,EC:FP7:PEOPLE,FP7-PEOPLE-2012-ITN,PNMR(2013), 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), and Università degli studi di Napoli Federico II

Subjects
[CHIM.THEO]Chemical Sciences/Theoretical and/or physical chemistry, magic-angle spinning, proton detection, solid-state NMR spectroscopy, resonance assignment
Abstract

International audience; Wir beschreiben die sensitive Messung von alpha-Protonen in voll protonierten Proteinen durch Festkörper-NMR mit Rotation um den magischen Winkel (MAS) von 100-111 kHz. Die exzellente Auflösung in der Cα-Hα-Ebene wird für 5 Proteine gezeigt, darunter Mikrokristalle, ein sedimentierter Komplex, ein Kapsid und Amyloidfibrillen. Ausgehend davon wurde ein Satz 3D-Spektren für die sequenzspezifische Zuordnung der Rückgrat- und der aliphatischen Seitenketten-Resonanzen entwickelt. Dabei wurden nur 500 μg Probe verwendet. Diese Entwicklungen beschleunigen strukturelle Untersuchungen von biomolekularen Komplexen, die nur in Submilligramm-Mengen verfügbar sind, ohne die Notwendigkeit einer Deuterierung.; We demonstrate sensitive detection of alpha protons of fully protonated proteins by solid-state NMR with 100-111 kHz magic-angle spinning (MAS). The excellent resolution in the Cα-Hα plane is demonstrated for 5 proteins, including microcrystals, a sedimented complex, a capsid and amyloid fibrils. A set of 3D spectra based on a Cα-Hα detection block was developed and applied for the sequence-specific backbone and aliphatic side-chain resonance assignment using only 500 μg of sample. These developments accelerate structural studies of biomolecular assemblies available in submilligram quantities without the need of protein deuteration.

Published
2016
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3. Temporal sweetness profile of MNEI protein in gelled model systems

Author

Di Monaco, Rossella, Galinanes Plaza, Adriana, Miele, Nicoletta A., Picone, Delia, Cavella, Silvana, Department of Agricultural Sciences, University of Naples Federico II, CAISIAL-Center of Food Innovation and Development in the Food Industry, Ingénierie, Procédés, Aliments (GENIAL), Institut National de la Recherche Agronomique (INRA)-AgroParisTech, Center for Food and Hospitality Research, Institut Paul Bocuse, Department of Chemical Sciences, 'Fondazione con il SUD' [[2011-PDR-19]], DI MONACO, Rossella, Galiñanes Plaza, Adriana, Miele, NICOLETTA ANTONELLA, Picone, Delia, Cavella, Silvana, and Edgar Chambers IV

Subjects
Food additive, Gel, Gelation, Algae, Sensory attribute, Protein, [SDV]Life Sciences [q-bio], digestive, oral, and skin physiology, Intensity profile, Innovative approache, food and beverages, Flavor perception, Time-intensity method, High-potency sweetener, Acidification, Scientific contribution, Solution, Beverage, Polysaccharide, Sugar substitute
Abstract

MNEI has been proved to be a high-potency sweetener that could be used in the beverage industry to satisfy consumer demands for low-caloric products. Until now its sweetness profile was studied only in liquid samples. So the objectives of this study were to characterize the sweetness intensity profile of MNEI protein in simple gelled systems, and to characterize the dominance sensation of more complex gelled systems in comparison with other sweeteners. First, the sweetness intensity of MNEI and of three commercial sweeteners (aspartame, saccharin, and sucrose) was determined in aqueous solutions and in gel, at different agar concentrations, by the time-Intensity method. Then, gels at 1.5% agar concentration, containing flavoring, coloring, and acidifying agent were evaluated using the temporal dominance of sensation method to study the interaction between sweetness and other sensory attributes. Differences regarding sweeteners in solutions and gels were reported showing a decrease of sweetness intensity perception when sweeteners were added in a gelled matrix, especially for MNEI. Additionally, MNEI seemed to be the sweetener most affected by all evaluation conditions (coloring and acidifying agents) in the TDS method. The results are an important scientific contribution to the knowledge of MNEI sensory profile in gelled and complex matrices that could increase its range of food applications. Practical applications: The use of both time intensity and temporal dominance of sensation methods in order to evaluate the temporal sweetness profile of MNEI-based gelled system represented a new approach in the study of sweet proteins. Indeed, the use of the TDS represented an innovative approach to study the effect of color on sweetness and flavor perception. According to our results, MNEI gels did not perform well comparing to the other sweeteners in semisolid matrix. However, further studies should be carried out in order to better understand the interaction between MNEI protein and the gelling as well as the coloring agents. Regarding the application in semisolid foods, it could be suggested the use of new technologies like encapsulation in order to protect the protein from experimental conditions and prevent its interaction with the sweet taste receptor.

Published
2016
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