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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....
Autores principales: | , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
2014
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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. |
format | Online Article Text |
id | pubmed-4216144 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2014 |
record_format | MEDLINE/PubMed |
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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