Chemical shift guided homology modeling of larger proteins

We describe an alternate approach to protein structure determination that relies on experimental NMR chemical shifts, plus sparse NOEs if available. The newly introduced alignment method, POMONA, directly exploits the powerful bioinformatics algorithms previously developed for sequence-based homolog...

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Detalles Bibliográficos
Autores principales: Shen, Yang, Bax, Ad
Formato: Online Artículo Texto
Lenguaje:English
Publicado: 2015
Materias:
Article
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4521993/
https://www.ncbi.nlm.nih.gov/pubmed/26053889
http://dx.doi.org/10.1038/nmeth.3437
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author Shen, Yang
Bax, Ad
author_facet Shen, Yang
Bax, Ad
author_sort Shen, Yang
collection PubMed
description We describe an alternate approach to protein structure determination that relies on experimental NMR chemical shifts, plus sparse NOEs if available. The newly introduced alignment method, POMONA, directly exploits the powerful bioinformatics algorithms previously developed for sequence-based homology modeling, but does not require significant sequence similarity. Protein templates, generated by POMONA, are subsequently used as input for chemical shift based Rosetta comparative modeling (CS-RosettaCM) to generate reliable full atom models.
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spelling pubmed-45219932016-01-31 Chemical shift guided homology modeling of larger proteins Shen, Yang Bax, Ad Nat Methods Article We describe an alternate approach to protein structure determination that relies on experimental NMR chemical shifts, plus sparse NOEs if available. The newly introduced alignment method, POMONA, directly exploits the powerful bioinformatics algorithms previously developed for sequence-based homology modeling, but does not require significant sequence similarity. Protein templates, generated by POMONA, are subsequently used as input for chemical shift based Rosetta comparative modeling (CS-RosettaCM) to generate reliable full atom models. 2015-06-08 2015-08 /pmc/articles/PMC4521993/ /pubmed/26053889 http://dx.doi.org/10.1038/nmeth.3437 Text en http://www.nature.com/authors/editorial_policies/license.html#terms Users may view, print, copy, and download text and data-mine the content in such documents, for the purposes of academic research, subject always to the full Conditions of use:http://www.nature.com/authors/editorial_policies/license.html#terms
spellingShingle Article
Shen, Yang
Bax, Ad
Chemical shift guided homology modeling of larger proteins
title Chemical shift guided homology modeling of larger proteins
title_full Chemical shift guided homology modeling of larger proteins
title_fullStr Chemical shift guided homology modeling of larger proteins
title_full_unstemmed Chemical shift guided homology modeling of larger proteins
title_short Chemical shift guided homology modeling of larger proteins
title_sort chemical shift guided homology modeling of larger proteins
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4521993/
https://www.ncbi.nlm.nih.gov/pubmed/26053889
http://dx.doi.org/10.1038/nmeth.3437
work_keys_str_mv AT shenyang chemicalshiftguidedhomologymodelingoflargerproteins
AT baxad chemicalshiftguidedhomologymodelingoflargerproteins

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