Zobrazeno 1 - 10
of 291
pro vyhledávání: '"Hermann E Gaub"'
Autor:
Steffen M Sedlak, Magnus S Bauer, Carleen Kluger, Leonard C Schendel, Lukas F Milles, Diana A Pippig, Hermann E Gaub
Publikováno v:
PLoS ONE, Vol 12, Iss 12, p e0188722 (2017)
The widely used interaction of the homotetramer streptavidin with the small molecule biotin has been intensively studied by force spectroscopy and has become a model system for receptor ligand interaction. However, streptavidin's tetravalency results
Externí odkaz:
https://doaj.org/article/82e31b451980452b9af828c2b63dc0d8
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:
PLoS ONE, Vol 9, Iss 2, p e89626 (2014)
Analysis of transcription factor binding to DNA sequences is of utmost importance to understand the intricate regulatory mechanisms that underlie gene expression. Several techniques exist that quantify DNA-protein affinity, but they are either very t
Externí odkaz:
https://doaj.org/article/8b53f41d9efc4a6da8144148aa084752
Autor:
Daniela Aschenbrenner, Diana A Pippig, Kamila Klamecka, Katja Limmer, Heinrich Leonhardt, Hermann E Gaub
Publikováno v:
PLoS ONE, Vol 9, Iss 12, p e115049 (2014)
Quantitative proteome research is greatly promoted by high-resolution parallel format assays. A characterization of protein complexes based on binding forces offers an unparalleled dynamic range and allows for the effective discrimination of non-spec
Externí odkaz:
https://doaj.org/article/f7dcdd0578f24543b56eb4c66798b25f
Autor:
Magnus S. Bauer, Sophia Gruber, Adina Hausch, Marcelo C.R. Melo, Priscila S.F.C. Gomes, Thomas Nicolaus, Lukas F. Milles, Hermann E. Gaub, Rafael C. Bernardi, Jan Lipfert
Viruses mutate under a variety of selection pressures, allowing them to continuously adapt to their hosts. Mutations in SARS-CoV-2 have shown effective evasion of population immunity and increased affinity to host factors, in particular to the cellul
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::6b68f93610cee19908aee682d4b7f321
https://doi.org/10.1101/2023.01.06.522349
https://doi.org/10.1101/2023.01.06.522349
Autor:
Yves F. Dufrêne, Gerhard Hummer, Cristina Lo Giudice, Hermann E. Gaub, David Alsteens, Peter Hinterdorfer, James J. De Yoreo, Andra C. Dumitru, Daniel J. Müller
Publikováno v:
Chemical Reviews, no. 121, p. 11701-11725 (2020)
During the last three decades, a series of key technological improvements turned atomic force microscopy (AFM) into a nanoscopic laboratory to directly observe and chemically characterize molecular and cell biological systems under physiological cond
Publikováno v:
Nanoscale. 12:6803-6809
The complex of the small molecule biotin and the homotetrameric protein streptavidin is key to a broad range of biotechnological applications. Therefore, the behavior of this extraordinarily high-affinity interaction under mechanical force is intensi
Autor:
Magnus S. Bauer, Sophia Gruber, Adina Hausch, Lukas F. Milles, Thomas Nicolaus, Leonard C. Schendel, Pilar López Navajas, Erik Procko, Daniel Lietha, Rafael C. Bernardi, Hermann E. Gaub, Jan Lipfert
Publikováno v:
Digital.CSIC. Repositorio Institucional del CSIC
instname
Digital.CSIC: Repositorio Institucional del CSIC
Consejo Superior de Investigaciones Científicas (CSIC)
instname
Digital.CSIC: Repositorio Institucional del CSIC
Consejo Superior de Investigaciones Científicas (CSIC)
SARS-CoV-2 infections are initiated by attachment of the receptor-binding domain (RBD) on the viral Spike protein to angiotensin-converting enzyme-2 (ACE2) on human host cells. This critical first step occurs in dynamic environments, where external f
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::9f2a4ab6fe9d91075750bc40e791c3d7
Publikováno v:
Nano Letters. 19:3176-3181
Since the development of the green fluorescent protein, fluorescent proteins (FP) are indispensable tools in molecular biology. Some FPs change their structure under illumination, which affects their interaction with other biomolecules or proteins. I
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