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NMR assignment of the nonstructural protein nsp3(1066–1181) from SARS-CoV

Sequence-specific NMR assignments of the globular core comprising the residues 1066–1181 within the non-structural protein nsp3e from the SARS coronavirus have been obtained using triple-resonance NMR experiments with the uniformly [(13)C, (15)N]-labeled protein. The backbone and side chain assignme...

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Detalles Bibliográficos
Autores principales: Serrano, Pedro, Johnson, Margaret A., Chatterjee, Amarnath, Pedrini, Bill, Wüthrich, Kurt
Formato: Texto
Lenguaje:English
Publicado: Springer Netherlands 2008
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2776825/
https://www.ncbi.nlm.nih.gov/pubmed/19636888
http://dx.doi.org/10.1007/s12104-008-9104-x
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author Serrano, Pedro
Johnson, Margaret A.
Chatterjee, Amarnath
Pedrini, Bill
Wüthrich, Kurt
author_facet Serrano, Pedro
Johnson, Margaret A.
Chatterjee, Amarnath
Pedrini, Bill
Wüthrich, Kurt
author_sort Serrano, Pedro
collection PubMed
description Sequence-specific NMR assignments of the globular core comprising the residues 1066–1181 within the non-structural protein nsp3e from the SARS coronavirus have been obtained using triple-resonance NMR experiments with the uniformly [(13)C, (15)N]-labeled protein. The backbone and side chain assignments are nearly complete, providing the basis for the ongoing NMR structure determination. A preliminary identification of regular secondary structures has been derived from the (13)C chemical shifts.
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spelling pubmed-27768252009-12-01 NMR assignment of the nonstructural protein nsp3(1066–1181) from SARS-CoV Serrano, Pedro Johnson, Margaret A. Chatterjee, Amarnath Pedrini, Bill Wüthrich, Kurt Biomol NMR Assign Article Sequence-specific NMR assignments of the globular core comprising the residues 1066–1181 within the non-structural protein nsp3e from the SARS coronavirus have been obtained using triple-resonance NMR experiments with the uniformly [(13)C, (15)N]-labeled protein. The backbone and side chain assignments are nearly complete, providing the basis for the ongoing NMR structure determination. A preliminary identification of regular secondary structures has been derived from the (13)C chemical shifts. Springer Netherlands 2008-07-22 2008 /pmc/articles/PMC2776825/ /pubmed/19636888 http://dx.doi.org/10.1007/s12104-008-9104-x Text en © Springer Science+Business Media B.V. 2008 This article is made available via the PMC Open Access Subset for unrestricted research re-use and secondary analysis in any form or by any means with acknowledgement of the original source. These permissions are granted for the duration of the World Health Organization (WHO) declaration of COVID-19 as a global pandemic.
spellingShingle Article
Serrano, Pedro
Johnson, Margaret A.
Chatterjee, Amarnath
Pedrini, Bill
Wüthrich, Kurt
NMR assignment of the nonstructural protein nsp3(1066–1181) from SARS-CoV
title NMR assignment of the nonstructural protein nsp3(1066–1181) from SARS-CoV
title_full NMR assignment of the nonstructural protein nsp3(1066–1181) from SARS-CoV
title_fullStr NMR assignment of the nonstructural protein nsp3(1066–1181) from SARS-CoV
title_full_unstemmed NMR assignment of the nonstructural protein nsp3(1066–1181) from SARS-CoV
title_short NMR assignment of the nonstructural protein nsp3(1066–1181) from SARS-CoV
title_sort nmr assignment of the nonstructural protein nsp3(1066–1181) from sars-cov
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2776825/
https://www.ncbi.nlm.nih.gov/pubmed/19636888
http://dx.doi.org/10.1007/s12104-008-9104-x
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