Zobrazeno 1 - 10
of 11
pro vyhledávání: '"Markus A. Jobst"'
Autor:
Markus A Jobst, Lukas F Milles, Constantin Schoeler, Wolfgang Ott, Daniel B Fried, Edward A Bayer, Hermann E Gaub, Michael A Nash
Publikováno v:
eLife, Vol 4 (2015)
Receptor-ligand pairs are ordinarily thought to interact through a lock and key mechanism, where a unique molecular conformation is formed upon binding. Contrary to this paradigm, cellulosomal cohesin-dockerin (Coh-Doc) pairs are believed to interact
Externí odkaz:
https://doaj.org/article/1a2462670b6c449891e5ed55c7da161f
Publikováno v:
Nanoscale. 11:407-411
Single-molecule cut-and-paste facilitates bottom-up directed assembly of nanoscale biomolecular networks in defined geometries and enables analysis with spatio-temporal resolution. However, arrangement of diverse molecules of interest requires versat
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::9a4cc3f42c16332aa64ccd2440466b81
https://doi.org/10.1039/c8nr08636b
https://doi.org/10.1039/c8nr08636b
Publikováno v:
Journal of Structural Biology. 197:3-12
Single-molecule force spectroscopy sheds light onto the free energy landscapes governing protein folding and molecular recognition. Since only a single molecule or single molecular complex is probed at any given point in time, the technique is capabl
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::6a420908a6a3dd1478d96d8bc452792a
https://doi.org/10.1016/j.jsb.2016.02.011
https://doi.org/10.1016/j.jsb.2016.02.011
Autor:
Lorenzo Rovigatti, Flavio Romano, Ard A. Louis, Markus A. Jobst, Martin Sajfutdinow, David M. Smith, Megan C. Engel, Tim Liedl, Jonathan P. K. Doye
Publikováno v:
ACS nano 12 (2018): 6734–6747. doi:10.1021/acsnano.8b01844
info:cnr-pdr/source/autori:Engel M.C.; Smith D.M.; Jobst M.A.; Sajfutdinow M.; Liedl T.; Romano F.; Rovigatti L.; Louis A.A.; Doye J.P.K./titolo:Force-Induced Unravelling of DNA Origami/doi:10.1021%2Facsnano.8b01844/rivista:ACS nano/anno:2018/pagina_da:6734/pagina_a:6747/intervallo_pagine:6734–6747/volume:12
info:cnr-pdr/source/autori:Engel M.C.; Smith D.M.; Jobst M.A.; Sajfutdinow M.; Liedl T.; Romano F.; Rovigatti L.; Louis A.A.; Doye J.P.K./titolo:Force-Induced Unravelling of DNA Origami/doi:10.1021%2Facsnano.8b01844/rivista:ACS nano/anno:2018/pagina_da:6734/pagina_a:6747/intervallo_pagine:6734–6747/volume:12
The mechanical properties of DNA nanostructures are of widespread interest as applications that exploit their stability under constant or intermittent external forces become increasingly common. We explore the force response of DNA origami in compreh
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e7ef0b434bee8042301830920d302747
http://hdl.handle.net/11573/1273784
http://hdl.handle.net/11573/1273784
Autor:
Michael A. Nash, Hermann E. Gaub, Markus A. Jobst, Magnus S. Bauer, Lukas F. Milles, Wolfgang Ott, Ellis Durner
Publikováno v:
ACS Nano
Single-molecule force spectroscopy (SMFS) is by now well established as a standard technique in biophysics and mechanobiology. In recent years, the technique has benefitted greatly from new approaches to bioconjugation of proteins to surfaces. Indeed
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::273407bbec5c4ce1849e9081838d6d23
https://pubmed.ncbi.nlm.nih.gov/28591514
https://pubmed.ncbi.nlm.nih.gov/28591514
Autor:
Markus A. Jobst, Constantin Schoeler, Hermann E. Gaub, Lukas F. Milles, Wolfgang Ott, Daniel B. Fried, Edward A. Bayer, Michael A. Nash
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::b18cb459e87cdbb9575bfb524fe14398
https://doi.org/10.7554/elife.10319.013
https://doi.org/10.7554/elife.10319.013
Autor:
Hermann E. Gaub, Edward A. Bayer, Michael A. Nash, Lukas F. Milles, Constantin Schoeler, Wolfgang Ott, Markus A. Jobst, Daniel B. Fried
Publikováno v:
eLife
eLife, Vol 4 (2015)
eLife, Vol 4 (2015)
Receptor-ligand pairs are ordinarily thought to interact through a lock and key mechanism, where a unique molecular conformation is formed upon binding. Contrary to this paradigm, cellulosomal cohesin-dockerin (Coh-Doc) pairs are believed to interact
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f4fb511d69a3d242ef4ec7c654ba4fda
http://europepmc.org/articles/PMC4728124
http://europepmc.org/articles/PMC4728124
Autor:
Hermann E. Gaub, Michael A. Nash, Markus A. Jobst, Marcus Otten, Lukas F. Milles, Tobias Verdorfer, Diana A. Pippig, Wolfgang Ott
Publikováno v:
Nature Methods
Nature methods
Nature methods
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 meas
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c31116231c5da760a0f2612e9e2a32cd
Autor:
Michael A. Nash, Klaus Schulten, Markus A. Jobst, Hermann E. Gaub, Ellis Durner, Wolfgang Ott, Daniel B. Fried, Constantin Schoeler, Klara H. Malinowska, Rafael C. Bernardi, Edward A. Bayer, Lukas F. Milles
Publikováno v:
Nature Communications
Challenging environments have guided nature in the development of ultrastable protein complexes. Specialized bacteria produce discrete multi-component protein networks called cellulosomes to effectively digest lignocellulosic biomass. While network a
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::87c8dfbf4e28c224896efd0ed1607524
https://pubmed.ncbi.nlm.nih.gov/25482395
https://pubmed.ncbi.nlm.nih.gov/25482395
Publikováno v:
Journal of Visualized Experiments
Cellulosomes are discrete multienzyme complexes used by a subset of anaerobic bacteria and fungi to digest lignocellulosic substrates. Assembly of the enzymes onto the noncatalytic scaffold protein is directed by interactions among a family of relate
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::9e90b677412493eaac4ad80cb6f33aca