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From Genes to Protein Mechanics on a Chip

Single-molecule force spectroscopy enables mechanical testing of individual proteins, however low experimental throughput limits the ability to screen constructs in parallel. We describe a microfluidic platform for on-chip protein expression and measurement of single-molecule mechanical properties....

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Detalles Bibliográficos
Autores principales: Otten, Marcus, Ott, Wolfgang, Jobst, Markus A., Milles, Lukas F., Verdorfer, Tobias, Pippig, Diana A., Nash, Michael A., Gaub, Hermann E.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: 2014
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4216144/
https://www.ncbi.nlm.nih.gov/pubmed/25194847
http://dx.doi.org/10.1038/nmeth.3099
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author Otten, Marcus
Ott, Wolfgang
Jobst, Markus A.
Milles, Lukas F.
Verdorfer, Tobias
Pippig, Diana A.
Nash, Michael A.
Gaub, Hermann E.
author_facet Otten, Marcus
Ott, Wolfgang
Jobst, Markus A.
Milles, Lukas F.
Verdorfer, Tobias
Pippig, Diana A.
Nash, Michael A.
Gaub, Hermann E.
author_sort Otten, Marcus
collection PubMed
description Single-molecule force spectroscopy enables mechanical testing of individual proteins, however low experimental throughput limits the ability to screen constructs in parallel. We describe a microfluidic platform for on-chip protein expression and measurement of single-molecule mechanical properties. We constructed microarrays of proteins covalently attached to a chip surface, and found that a single cohesin-modified cantilever that bound to the terminal dockerin-tag of each protein remained stable over thousands of pulling cycles. The ability to synthesize and mechanically probe protein libraries presents new opportunities for high-throughput mechanical phenotyping.
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spelling pubmed-42161442015-05-01 From Genes to Protein Mechanics on a Chip Otten, Marcus Ott, Wolfgang Jobst, Markus A. Milles, Lukas F. Verdorfer, Tobias Pippig, Diana A. Nash, Michael A. Gaub, Hermann E. Nat Methods Article Single-molecule force spectroscopy enables mechanical testing of individual proteins, however low experimental throughput limits the ability to screen constructs in parallel. We describe a microfluidic platform for on-chip protein expression and measurement of single-molecule mechanical properties. We constructed microarrays of proteins covalently attached to a chip surface, and found that a single cohesin-modified cantilever that bound to the terminal dockerin-tag of each protein remained stable over thousands of pulling cycles. The ability to synthesize and mechanically probe protein libraries presents new opportunities for high-throughput mechanical phenotyping. 2014-09-07 2014-11 /pmc/articles/PMC4216144/ /pubmed/25194847 http://dx.doi.org/10.1038/nmeth.3099 Text en 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
Otten, Marcus
Ott, Wolfgang
Jobst, Markus A.
Milles, Lukas F.
Verdorfer, Tobias
Pippig, Diana A.
Nash, Michael A.
Gaub, Hermann E.
From Genes to Protein Mechanics on a Chip
title From Genes to Protein Mechanics on a Chip
title_full From Genes to Protein Mechanics on a Chip
title_fullStr From Genes to Protein Mechanics on a Chip
title_full_unstemmed From Genes to Protein Mechanics on a Chip
title_short From Genes to Protein Mechanics on a Chip
title_sort from genes to protein mechanics on a chip
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4216144/
https://www.ncbi.nlm.nih.gov/pubmed/25194847
http://dx.doi.org/10.1038/nmeth.3099
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