ParkinsonFranceV1, Hal, Checkpoint, bibRecord, 000055

Further exploration of the conformational space of α-synuclein fibrils: solid-state NMR assignment of a high-pH polymorph.

Identifieur interne : 000055 ( Hal/Checkpoint ); précédent : 000054; suivant : 000056

Further exploration of the conformational space of α-synuclein fibrils: solid-state NMR assignment of a high-pH polymorph.

Auteurs : Joeri Verasdonck [Suisse] ; Luc Bousset [France] ; Julia Gath [Suisse] ; Ronald Melki [France] ; Anja Böckmann [France] ; Beat H. Meier [Suisse]

Source :

Biomolecular NMR Assignments [ 1874-270X ] ; 2016-04-04.

RBID : Hal:hal-01240180

English descriptors

mix :
- Polymorphism , Synuclein, Solid-state NMR .

Abstract

Polymorphism is a common and important phenomenon for protein fibrils which has been linked to the appearance of strains in prion and other neurodegenerative diseases. Parkinson disease is a frequently occurring neurodegenerative pathology, tightly associated with the formation of Lewy bodies. These deposits mainly consist of α-synuclein in fibrillar, β-sheet-rich form. α-synuclein is known to form numerous different polymorphs, which show distinct structural features. Here, we describe the chemical shift assignments, and derive the secondary structure, of a polymorph that was fibrillized at higher-than-physiological pH conditions. The fibrillar core contains residues 40–95, with both the C- and N-terminus not showing any ordered, rigid parts. The chemical shifts are similar to those recorded previously for an assigned polymorph that was fibrillized at neutral pH.

Url:

https://hal.archives-ouvertes.fr/hal-01240180

DOI: 10.1007/s12104-015-9628-9

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

to stream Hal, to step Corpus: 000487
to stream Hal, to step Curation: 000487

Links to Exploration step

Hal:hal-01240180

Le document en format XML

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<front><div type="abstract" xml:lang="en">Polymorphism is a common and important phenomenon for protein fibrils which has been linked to the appearance of strains in prion and other neurodegenerative diseases. Parkinson disease is a frequently occurring neurodegenerative pathology, tightly associated with the formation of Lewy bodies. These deposits mainly consist of α-synuclein in fibrillar, β-sheet-rich form. α-synuclein is known to form numerous different polymorphs, which show distinct structural features. Here, we describe the chemical shift assignments, and derive the secondary structure, of a polymorph that was fibrillized at higher-than-physiological pH conditions. The fibrillar core contains residues 40–95, with both the C- and N-terminus not showing any ordered, rigid parts. The chemical shifts are similar to those recorded previously for an assigned polymorph that was fibrillized at neutral pH.</div>
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          <sourceDesc>            <biblStruct>              <analytic>                <title xml:lang="en">Further exploration of the conformational space of α-synuclein fibrils: solid-state NMR assignment of a high-pH polymorph.</title>
                <author role="aut">                  <persName>                    <forename type="first">Joeri</forename>
                    <surname>Verasdonck</surname>
                  </persName>
                  <idno type="halauthorid">1257860</idno>
                  <affiliation ref="#struct-425064"></affiliation>
                </author>
                <author role="aut">                  <persName>                    <forename type="first">Luc</forename>
                    <surname>Bousset</surname>
                  </persName>
                  <idno type="halauthorid">190085</idno>
                  <affiliation ref="#struct-418266"></affiliation>
                </author>
                <author role="aut">                  <persName>                    <forename type="first">Julia</forename>
                    <surname>Gath</surname>
                  </persName>
                  <idno type="halauthorid">1193542</idno>
                  <affiliation ref="#struct-425064"></affiliation>
                </author>
                <author role="aut">                  <persName>                    <forename type="first">Ronald</forename>
                    <surname>Melki</surname>
                  </persName>
                  <idno type="halauthorid">190086</idno>
                  <affiliation ref="#struct-418266"></affiliation>
                </author>
                <author role="aut">                  <persName>                    <forename type="first">Anja</forename>
                    <surname>Böckmann</surname>
                  </persName>
                  <idno type="halauthorid">104714</idno>
                  <affiliation ref="#struct-227725"></affiliation>
                </author>
                <author role="aut">                  <persName>                    <forename type="first">Beat H</forename>
                    <surname>Meier</surname>
                  </persName>
                  <idno type="halauthorid">815982</idno>
                  <affiliation ref="#struct-425064"></affiliation>
                </author>
              </analytic>
              <monogr>                <idno type="halJournalId" status="VALID">53896</idno>
                <idno type="issn">1874-270X</idno>
                <title level="j">Biomolecular NMR Assignments</title>
                <imprint>                  <publisher>Springer</publisher>
                  <biblScope unit="volume">10</biblScope>
                  <biblScope unit="issue">1</biblScope>
                  <biblScope unit="pp">5-12</biblScope>
                  <date type="datePub">2016-04-04</date>
                </imprint>
              </monogr>
              <idno type="doi">10.1007/s12104-015-9628-9</idno>
              <idno type="pubmed">26318307</idno>
            </biblStruct>
          </sourceDesc>
          <profileDesc>            <langUsage>              <language ident="en">English</language>
            </langUsage>
            <textClass>              <keywords scheme="author">                <term xml:lang="en"> Synuclein</term>
                <term xml:lang="en"> Polymorphism </term>
                <term xml:lang="en">Solid-state NMR </term>
              </keywords>
              <classCode scheme="halDomain" n="sdv.neu.nb">Life Sciences [q-bio]/Neurons and Cognition [q-bio.NC]/Neurobiology</classCode>
              <classCode scheme="halDomain" n="sdv.neu.pc">Life Sciences [q-bio]/Neurons and Cognition [q-bio.NC]/Psychology and behavior</classCode>
              <classCode scheme="halDomain" n="sdv.neu.sc">Life Sciences [q-bio]/Neurons and Cognition [q-bio.NC]/Cognitive Sciences</classCode>
              <classCode scheme="halTypology" n="ART">Journal articles</classCode>
            </textClass>
            <abstract xml:lang="en">Polymorphism is a common and important phenomenon for protein fibrils which has been linked to the appearance of strains in prion and other neurodegenerative diseases. Parkinson disease is a frequently occurring neurodegenerative pathology, tightly associated with the formation of Lewy bodies. These deposits mainly consist of α-synuclein in fibrillar, β-sheet-rich form. α-synuclein is known to form numerous different polymorphs, which show distinct structural features. Here, we describe the chemical shift assignments, and derive the secondary structure, of a polymorph that was fibrillized at higher-than-physiological pH conditions. The fibrillar core contains residues 40–95, with both the C- and N-terminus not showing any ordered, rigid parts. The chemical shifts are similar to those recorded previously for an assigned polymorph that was fibrillized at neutral pH.</abstract>
          </profileDesc>
        </hal>
</record>

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	La maladie de Parkinson en France (serveur d'exploration)
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La maladie de Parkinson en France (serveur d'exploration)

Further exploration of the conformational space of α-synuclein fibrils: solid-state NMR assignment of a high-pH polymorph.

Further exploration of the conformational space of α-synuclein fibrils: solid-state NMR assignment of a high-pH polymorph.

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