Engineered Nanostructured β-Sheet Peptides Protect Membrane Proteins

We have designed β-strand peptides (BP) that stabilize integral membrane proteins (IMP). BPs self-assemble in solution as filaments and become restructured upon association with IMPs; the resulting IMP/BP complexes resist aggregation when diluted in detergent-free buffer and are examined as stable,...

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Autores principales: Tao, Houchao, Lee, Sung Chang, Moeller, Arne, Roy, Rituparna Sinha, Siu, Fai Yiu, Zimmermann, Jörg, Stevens, Raymond C., Potter, Clinton S., Carragher, Bridget, Zhang, Qinghai
Formato: Online Artículo Texto
Lenguaje:English
Publicado: 2013
Materias:
Article
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3753066/
https://www.ncbi.nlm.nih.gov/pubmed/23817067
http://dx.doi.org/10.1038/nmeth.2533
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author Tao, Houchao
Lee, Sung Chang
Moeller, Arne
Roy, Rituparna Sinha
Siu, Fai Yiu
Zimmermann, Jörg
Stevens, Raymond C.
Potter, Clinton S.
Carragher, Bridget
Zhang, Qinghai
author_facet Tao, Houchao
Lee, Sung Chang
Moeller, Arne
Roy, Rituparna Sinha
Siu, Fai Yiu
Zimmermann, Jörg
Stevens, Raymond C.
Potter, Clinton S.
Carragher, Bridget
Zhang, Qinghai
author_sort Tao, Houchao
collection PubMed
description We have designed β-strand peptides (BP) that stabilize integral membrane proteins (IMP). BPs self-assemble in solution as filaments and become restructured upon association with IMPs; the resulting IMP/BP complexes resist aggregation when diluted in detergent-free buffer and are examined as stable, single particles with low detergent background by electron microscopy. This enables clear visualization of a spectrum of flexible conformations in the highly dynamic ATP-binding cassette (ABC) transporter MsbA.
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spelling pubmed-37530662014-02-01 Engineered Nanostructured β-Sheet Peptides Protect Membrane Proteins Tao, Houchao Lee, Sung Chang Moeller, Arne Roy, Rituparna Sinha Siu, Fai Yiu Zimmermann, Jörg Stevens, Raymond C. Potter, Clinton S. Carragher, Bridget Zhang, Qinghai Nat Methods Article We have designed β-strand peptides (BP) that stabilize integral membrane proteins (IMP). BPs self-assemble in solution as filaments and become restructured upon association with IMPs; the resulting IMP/BP complexes resist aggregation when diluted in detergent-free buffer and are examined as stable, single particles with low detergent background by electron microscopy. This enables clear visualization of a spectrum of flexible conformations in the highly dynamic ATP-binding cassette (ABC) transporter MsbA. 2013-06-30 2013-08 /pmc/articles/PMC3753066/ /pubmed/23817067 http://dx.doi.org/10.1038/nmeth.2533 Text en Users may view, print, copy, download and 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
Tao, Houchao
Lee, Sung Chang
Moeller, Arne
Roy, Rituparna Sinha
Siu, Fai Yiu
Zimmermann, Jörg
Stevens, Raymond C.
Potter, Clinton S.
Carragher, Bridget
Zhang, Qinghai
Engineered Nanostructured β-Sheet Peptides Protect Membrane Proteins
title Engineered Nanostructured β-Sheet Peptides Protect Membrane Proteins
title_full Engineered Nanostructured β-Sheet Peptides Protect Membrane Proteins
title_fullStr Engineered Nanostructured β-Sheet Peptides Protect Membrane Proteins
title_full_unstemmed Engineered Nanostructured β-Sheet Peptides Protect Membrane Proteins
title_short Engineered Nanostructured β-Sheet Peptides Protect Membrane Proteins
title_sort engineered nanostructured β-sheet peptides protect membrane proteins
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3753066/
https://www.ncbi.nlm.nih.gov/pubmed/23817067
http://dx.doi.org/10.1038/nmeth.2533
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