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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...
Autores principales: | , , , , |
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Formato: | Texto |
Lenguaje: | English |
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Springer Netherlands
2008
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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. |
format | Text |
id | pubmed-2776825 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2008 |
publisher | Springer Netherlands |
record_format | MEDLINE/PubMed |
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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