PittsburghV1, France, Analysis, bibRecord, 000036

Expanding the horizons for structural analysis of fully protonated protein assemblies by NMR spectroscopy at MAS frequencies above 100 kHz

Identifieur interne : 000036 ( France/Analysis ); précédent : 000035; suivant : 000037

Expanding the horizons for structural analysis of fully protonated protein assemblies by NMR spectroscopy at MAS frequencies above 100 kHz

Auteurs : Jochem Struppe [États-Unis] ; Caitlin M. Quinn [États-Unis] ; Manman Lu [États-Unis] ; Mingzhang Wang [États-Unis] ; Guangjin Hou [États-Unis] ; Xingyu Lu [États-Unis] ; Jodi Kraus [États-Unis] ; Loren B. Andreas [France] ; Jan Stanek [France] ; Daniela Lalli [France] ; Anne Lesage [France] ; Guido Pintacuda [France] ; Werner Maas [États-Unis] ; Angela M. Gronenborn [États-Unis] ; Tatyana Polenova [États-Unis]

Source :

Solid State Nuclear Magnetic Resonance [ 0926-2040 ] ; 2017.

RBID : Hal:hal-01575525

English descriptors

mix :
- MAS NMR, Protein assemblies, Proton-detected MAS NMR correlations, HIV-1 capsid protein.

Abstract

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.

Url:

https://hal.archives-ouvertes.fr/hal-01575525

DOI: 10.1016/j.ssnmr.2017.07.001

Affiliations:

Links toward previous steps (curation, corpus...)

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Links to Exploration step

Hal:hal-01575525

Le document en format XML

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<author><name sortKey="Lesage, Anne" sort="Lesage, Anne" uniqKey="Lesage A" first="Anne" last="Lesage">Anne Lesage</name>
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<author><name sortKey="Pintacuda, Guido" sort="Pintacuda, Guido" uniqKey="Pintacuda G" first="Guido" last="Pintacuda">Guido Pintacuda</name>
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<country>France</country>
<placeName><settlement type="city">Lyon</settlement>
<region type="region" nuts="2">Auvergne-Rhône-Alpes</region>
<region type="old region" nuts="2">Rhône-Alpes</region>
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<orgName type="institution" wicri:auto="newGroup">Université de Lyon</orgName>
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</author>
<author><name sortKey="Maas, Werner" sort="Maas, Werner" uniqKey="Maas W" first="Werner" last="Maas">Werner Maas</name>
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          <desc>            <address>              <addrLine>Billerica, Massachusetts 01821, United States</addrLine>
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</hal:affiliation>
<country>États-Unis</country>
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</author>
<author><name sortKey="Gronenborn, Angela M" sort="Gronenborn, Angela M" uniqKey="Gronenborn A" first="Angela M." last="Gronenborn">Angela M. Gronenborn</name>
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          </desc>
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<country>États-Unis</country>
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<author><name sortKey="Polenova, Tatyana" sort="Polenova, Tatyana" uniqKey="Polenova T" first="Tatyana" last="Polenova">Tatyana Polenova</name>
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          <desc>            <address>              <addrLine>University of Delaware, Newark, Delaware 19716, United States</addrLine>
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          <desc>            <address>              <addrLine>Newark, DE 19716 USA</addrLine>
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            <ref type="url">http://www.udel.edu/</ref>
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<country>États-Unis</country>
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<idno type="DOI">10.1016/j.ssnmr.2017.07.001</idno>
<series><title level="j">Solid State Nuclear Magnetic Resonance</title>
<idno type="ISSN">0926-2040</idno>
<imprint><date type="datePub">2017</date>
</imprint>
</series>
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</sourceDesc>
</fileDesc>
<profileDesc><textClass><keywords scheme="mix" xml:lang="en"><term> MAS NMR</term>
<term> Protein assemblies</term>
<term> Proton-detected MAS NMR correlations</term>
<term>HIV-1 capsid protein</term>
</keywords>
</textClass>
</profileDesc>
</teiHeader>
<front><div type="abstract" xml:lang="en">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.</div>
</front>
</TEI>
<affiliations><list><country><li>France</li>
<li>États-Unis</li>
</country>
<region><li>Auvergne-Rhône-Alpes</li>
<li>Rhône-Alpes</li>
</region>
<settlement><li>Lyon</li>
</settlement>
<orgName><li>Université Claude Bernard Lyon 1</li>
<li>Université de Lyon</li>
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</list>
<tree><country name="États-Unis"><noRegion><name sortKey="Struppe, Jochem" sort="Struppe, Jochem" uniqKey="Struppe J" first="Jochem" last="Struppe">Jochem Struppe</name>
</noRegion>
<name sortKey="Gronenborn, Angela M" sort="Gronenborn, Angela M" uniqKey="Gronenborn A" first="Angela M." last="Gronenborn">Angela M. Gronenborn</name>
<name sortKey="Hou, Guangjin" sort="Hou, Guangjin" uniqKey="Hou G" first="Guangjin" last="Hou">Guangjin Hou</name>
<name sortKey="Kraus, Jodi" sort="Kraus, Jodi" uniqKey="Kraus J" first="Jodi" last="Kraus">Jodi Kraus</name>
<name sortKey="Lu, Manman" sort="Lu, Manman" uniqKey="Lu M" first="Manman" last="Lu">Manman Lu</name>
<name sortKey="Lu, Xingyu" sort="Lu, Xingyu" uniqKey="Lu X" first="Xingyu" last="Lu">Xingyu Lu</name>
<name sortKey="Maas, Werner" sort="Maas, Werner" uniqKey="Maas W" first="Werner" last="Maas">Werner Maas</name>
<name sortKey="Polenova, Tatyana" sort="Polenova, Tatyana" uniqKey="Polenova T" first="Tatyana" last="Polenova">Tatyana Polenova</name>
<name sortKey="Quinn, Caitlin M" sort="Quinn, Caitlin M" uniqKey="Quinn C" first="Caitlin M." last="Quinn">Caitlin M. Quinn</name>
<name sortKey="Wang, Mingzhang" sort="Wang, Mingzhang" uniqKey="Wang M" first="Mingzhang" last="Wang">Mingzhang Wang</name>
</country>
<country name="France"><region name="Auvergne-Rhône-Alpes"><name sortKey="Andreas, Loren B" sort="Andreas, Loren B" uniqKey="Andreas L" first="Loren B." last="Andreas">Loren B. Andreas</name>
</region>
<name sortKey="Lalli, Daniela" sort="Lalli, Daniela" uniqKey="Lalli D" first="Daniela" last="Lalli">Daniela Lalli</name>
<name sortKey="Lesage, Anne" sort="Lesage, Anne" uniqKey="Lesage A" first="Anne" last="Lesage">Anne Lesage</name>
<name sortKey="Pintacuda, Guido" sort="Pintacuda, Guido" uniqKey="Pintacuda G" first="Guido" last="Pintacuda">Guido Pintacuda</name>
<name sortKey="Stanek, Jan" sort="Stanek, Jan" uniqKey="Stanek J" first="Jan" last="Stanek">Jan Stanek</name>
</country>
</tree>
</affiliations>
</record>

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Expanding the horizons for structural analysis of fully protonated protein assemblies by NMR spectroscopy at MAS frequencies above 100 kHz

Expanding the horizons for structural analysis of fully protonated protein assemblies by NMR spectroscopy at MAS frequencies above 100 kHz

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