Real-time monitoring of protein complexes reveals their quaternary organization and dynamics.
The dynamics of protein complexes are crucial for their function yet are challenging to study. Here, we present a nanoelectrospray (nESI) mass spectrometry (MS) approach capable of simultaneously providing structural and dynamical information for protein complexes. We investigate the properties of t...
| Principais autores: | , , , , , |
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| Formato: | Journal article |
| Idioma: | English |
| Publicado em: |
2008
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| _version_ | 1826257535750897664 |
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| author | Painter, A Jaya, N Basha, E Vierling, E Robinson, C Benesch, J |
| author_facet | Painter, A Jaya, N Basha, E Vierling, E Robinson, C Benesch, J |
| author_sort | Painter, A |
| collection | OXFORD |
| description | The dynamics of protein complexes are crucial for their function yet are challenging to study. Here, we present a nanoelectrospray (nESI) mass spectrometry (MS) approach capable of simultaneously providing structural and dynamical information for protein complexes. We investigate the properties of two small heat shock proteins (sHSPs) and find that these proteins exist as dodecamers composed of dimeric building blocks. Moreover, we show that these proteins exchange dimers on the timescale of minutes, with the rate of exchange being strongly temperature dependent. Because these proteins are expressed in the same cellular compartment, we anticipate that this dynamical behavior is crucial to their function in vivo. Furthermore, we propose that the approach used here is applicable to a range of nonequilibrium systems and is capable of providing both structural and dynamical information necessary for functional genomics. |
| first_indexed | 2024-03-06T18:19:46Z |
| format | Journal article |
| id | oxford-uuid:05dcc5aa-45ea-4b8a-b559-50aeca99b501 |
| institution | University of Oxford |
| language | English |
| last_indexed | 2024-03-06T18:19:46Z |
| publishDate | 2008 |
| record_format | dspace |
| spelling | oxford-uuid:05dcc5aa-45ea-4b8a-b559-50aeca99b5012022-03-26T08:59:32ZReal-time monitoring of protein complexes reveals their quaternary organization and dynamics.Journal articlehttp://purl.org/coar/resource_type/c_dcae04bcuuid:05dcc5aa-45ea-4b8a-b559-50aeca99b501EnglishSymplectic Elements at Oxford2008Painter, AJaya, NBasha, EVierling, ERobinson, CBenesch, JThe dynamics of protein complexes are crucial for their function yet are challenging to study. Here, we present a nanoelectrospray (nESI) mass spectrometry (MS) approach capable of simultaneously providing structural and dynamical information for protein complexes. We investigate the properties of two small heat shock proteins (sHSPs) and find that these proteins exist as dodecamers composed of dimeric building blocks. Moreover, we show that these proteins exchange dimers on the timescale of minutes, with the rate of exchange being strongly temperature dependent. Because these proteins are expressed in the same cellular compartment, we anticipate that this dynamical behavior is crucial to their function in vivo. Furthermore, we propose that the approach used here is applicable to a range of nonequilibrium systems and is capable of providing both structural and dynamical information necessary for functional genomics. |
| spellingShingle | Painter, A Jaya, N Basha, E Vierling, E Robinson, C Benesch, J Real-time monitoring of protein complexes reveals their quaternary organization and dynamics. |
| title | Real-time monitoring of protein complexes reveals their quaternary organization and dynamics. |
| title_full | Real-time monitoring of protein complexes reveals their quaternary organization and dynamics. |
| title_fullStr | Real-time monitoring of protein complexes reveals their quaternary organization and dynamics. |
| title_full_unstemmed | Real-time monitoring of protein complexes reveals their quaternary organization and dynamics. |
| title_short | Real-time monitoring of protein complexes reveals their quaternary organization and dynamics. |
| title_sort | real time monitoring of protein complexes reveals their quaternary organization and dynamics |
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