Cargando…

Kinetic analysis of protein aggregation monitored by real-time 2D solid-state NMR spectroscopy

It is shown that real-time 2D solid-state NMR can be used to obtain kinetic and structural information about the process of protein aggregation. In addition to the incorporation of kinetic information involving intermediate states, this approach can offer atom-specific resolution for all detectable...

Descripción completa

Detalles Bibliográficos
Autores principales: Etzkorn, Manuel, Böckmann, Anja, Baldus, Marc
Formato: Texto
Lenguaje:English
Publicado: Springer Netherlands 2011
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3042102/
https://www.ncbi.nlm.nih.gov/pubmed/21253842
http://dx.doi.org/10.1007/s10858-011-9468-6
_version_ 1782198511010316288
author Etzkorn, Manuel
Böckmann, Anja
Baldus, Marc
author_facet Etzkorn, Manuel
Böckmann, Anja
Baldus, Marc
author_sort Etzkorn, Manuel
collection PubMed
description It is shown that real-time 2D solid-state NMR can be used to obtain kinetic and structural information about the process of protein aggregation. In addition to the incorporation of kinetic information involving intermediate states, this approach can offer atom-specific resolution for all detectable species. The analysis was carried out using experimental data obtained during aggregation of the 10.4 kDa Crh protein, which has been shown to involve a partially unfolded intermediate state prior to aggregation. Based on a single real-time 2D (13)C–(13)C transition spectrum, kinetic information about the refolding and aggregation step could be extracted. In addition, structural rearrangements associated with refolding are estimated and several different aggregation scenarios were compared to the experimental data.
format Text
id pubmed-3042102
institution National Center for Biotechnology Information
language English
publishDate 2011
publisher Springer Netherlands
record_format MEDLINE/PubMed
spelling pubmed-30421022011-03-29 Kinetic analysis of protein aggregation monitored by real-time 2D solid-state NMR spectroscopy Etzkorn, Manuel Böckmann, Anja Baldus, Marc J Biomol NMR Article It is shown that real-time 2D solid-state NMR can be used to obtain kinetic and structural information about the process of protein aggregation. In addition to the incorporation of kinetic information involving intermediate states, this approach can offer atom-specific resolution for all detectable species. The analysis was carried out using experimental data obtained during aggregation of the 10.4 kDa Crh protein, which has been shown to involve a partially unfolded intermediate state prior to aggregation. Based on a single real-time 2D (13)C–(13)C transition spectrum, kinetic information about the refolding and aggregation step could be extracted. In addition, structural rearrangements associated with refolding are estimated and several different aggregation scenarios were compared to the experimental data. Springer Netherlands 2011-01-21 2011 /pmc/articles/PMC3042102/ /pubmed/21253842 http://dx.doi.org/10.1007/s10858-011-9468-6 Text en © The Author(s) 2011 https://creativecommons.org/licenses/by-nc/4.0/ This article is distributed under the terms of the Creative Commons Attribution Noncommercial License which permits any noncommercial use, distribution, and reproduction in any medium, provided the original author(s) and source are credited.
spellingShingle Article
Etzkorn, Manuel
Böckmann, Anja
Baldus, Marc
Kinetic analysis of protein aggregation monitored by real-time 2D solid-state NMR spectroscopy
title Kinetic analysis of protein aggregation monitored by real-time 2D solid-state NMR spectroscopy
title_full Kinetic analysis of protein aggregation monitored by real-time 2D solid-state NMR spectroscopy
title_fullStr Kinetic analysis of protein aggregation monitored by real-time 2D solid-state NMR spectroscopy
title_full_unstemmed Kinetic analysis of protein aggregation monitored by real-time 2D solid-state NMR spectroscopy
title_short Kinetic analysis of protein aggregation monitored by real-time 2D solid-state NMR spectroscopy
title_sort kinetic analysis of protein aggregation monitored by real-time 2d solid-state nmr spectroscopy
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3042102/
https://www.ncbi.nlm.nih.gov/pubmed/21253842
http://dx.doi.org/10.1007/s10858-011-9468-6
work_keys_str_mv AT etzkornmanuel kineticanalysisofproteinaggregationmonitoredbyrealtime2dsolidstatenmrspectroscopy
AT bockmannanja kineticanalysisofproteinaggregationmonitoredbyrealtime2dsolidstatenmrspectroscopy
AT baldusmarc kineticanalysisofproteinaggregationmonitoredbyrealtime2dsolidstatenmrspectroscopy