Zobrazeno 1 - 10
of 10
pro vyhledávání: '"Constantin Schoeler"'
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:
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
Autor:
Zaida Luthey-Schulten, Constantin Schoeler, Ellis Durner, Michael A. Nash, Hermann E. Gaub, Edward A. Bayer, Klara H. Malinowska, Rafael C. Bernardi, Bruna Gregatti de Carvalho
Publikováno v:
Journal of the American Chemical Society
Can molecular dynamics simulations predict the mechanical behavior of protein complexes? Can simulations decipher the role of protein domains of unknown function in large macromolecular complexes? Here, we employ a wide-sampling computational approac
Protein receptor-ligand pairs are increasingly used as specific molecular handles in single-molecule protein-unfolding experiments. Further, known marker domains, also referred to as fingerprints, provide unique unfolding signatures to identify speci
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::74d399a3702a11d83ce9f1b3a4a21806
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
Autor:
Constantin Schoeler, Hermann E. Gaub, Ellis Durner, Wolfgang Ott, Klara H. Malinowska, Rafael C. Bernardi, Edward A. Bayer, Michael A. Nash, Klaus Schulten
Here we employed single-molecule force spectroscopy with an atomic force microscope (AFM) and steered molecular dynamics (SMD) simulations to reveal force propagation pathways through a mechanically ultrastable multi-domain cellulosome protein comple
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::40792caf9a40111fbe4189175f892a2d
https://europepmc.org/articles/PMC4721519/
https://europepmc.org/articles/PMC4721519/
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
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
Autor:
Constantin Schoeler, RafaelC. Bernardi, Klara H. Malinowska, Ellis Durner, Wolfgang Ott, Edward A. Bayer, Klaus Schulten, Michael A. Nash, Hermann E. Gaub
Publikováno v:
Nano Letters; Nov2015, Vol. 15 Issue 11, p7370-7376, 7p