Mass spectrometry captures structural intermediates in protein fiber self-assembly

Self-assembling proteins, the basis for a broad range of biological scaffolds, are challenging to study using most structural biology approaches. Here we show that mass spectrometry (MS) in combination with MD simulations captures structural features of short-lived oligomeric intermediates in spider...

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Detalles Bibliográficos
Autores principales: Landreh, Michael, Andersson, Marlene, Marklund, Erik G., Jia, Qiupin, Meng, Qing, Johansson, Jan, Robinson, Carol V., Rising, Anna
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Royal Society of Chemistry 2017
Materias:
Chemistry
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5530726/
https://www.ncbi.nlm.nih.gov/pubmed/28184384
http://dx.doi.org/10.1039/c7cc00307b
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author Landreh, Michael
Andersson, Marlene
Marklund, Erik G.
Jia, Qiupin
Meng, Qing
Johansson, Jan
Robinson, Carol V.
Rising, Anna
author_facet Landreh, Michael
Andersson, Marlene
Marklund, Erik G.
Jia, Qiupin
Meng, Qing
Johansson, Jan
Robinson, Carol V.
Rising, Anna
author_sort Landreh, Michael
collection PubMed
description Self-assembling proteins, the basis for a broad range of biological scaffolds, are challenging to study using most structural biology approaches. Here we show that mass spectrometry (MS) in combination with MD simulations captures structural features of short-lived oligomeric intermediates in spider silk formation, providing direct insights into its complex assembly process.
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spelling pubmed-55307262017-08-14 Mass spectrometry captures structural intermediates in protein fiber self-assembly Landreh, Michael Andersson, Marlene Marklund, Erik G. Jia, Qiupin Meng, Qing Johansson, Jan Robinson, Carol V. Rising, Anna Chem Commun (Camb) Chemistry Self-assembling proteins, the basis for a broad range of biological scaffolds, are challenging to study using most structural biology approaches. Here we show that mass spectrometry (MS) in combination with MD simulations captures structural features of short-lived oligomeric intermediates in spider silk formation, providing direct insights into its complex assembly process. Royal Society of Chemistry 2017-03-21 2017-02-01 /pmc/articles/PMC5530726/ /pubmed/28184384 http://dx.doi.org/10.1039/c7cc00307b Text en This journal is © The Royal Society of Chemistry 2017 http://creativecommons.org/licenses/by/3.0/ This is an Open Access article distributed under the terms of the Creative Commons Attribution 3.0 Unported License (http://creativecommons.org/licenses/by/3.0/) which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.
spellingShingle Chemistry
Landreh, Michael
Andersson, Marlene
Marklund, Erik G.
Jia, Qiupin
Meng, Qing
Johansson, Jan
Robinson, Carol V.
Rising, Anna
Mass spectrometry captures structural intermediates in protein fiber self-assembly
title Mass spectrometry captures structural intermediates in protein fiber self-assembly
title_full Mass spectrometry captures structural intermediates in protein fiber self-assembly
title_fullStr Mass spectrometry captures structural intermediates in protein fiber self-assembly
title_full_unstemmed Mass spectrometry captures structural intermediates in protein fiber self-assembly
title_short Mass spectrometry captures structural intermediates in protein fiber self-assembly
title_sort mass spectrometry captures structural intermediates in protein fiber self-assembly
topic Chemistry
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5530726/
https://www.ncbi.nlm.nih.gov/pubmed/28184384
http://dx.doi.org/10.1039/c7cc00307b
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