Zobrazeno 1 - 6
of 6
pro vyhledávání: '"Marc Löllmann"'
Autor:
Sören Doose, Markus Sauer, Lilly Nagel, Marc Löllmann, Norbert Sewald, Anne Burgert, Carolin Plattner, Stefan Bollmann
Publikováno v:
Chemphyschem : a European journal of chemical physics and physical chemistry. 12(16)
With a twist: The conformational dynamics of glycosylated glycine–serine peptides is studied using contact- induced fluorescence quenching analysed by fluorescence correlation spectroscopy. End-to-end contact rates on ns–μs timescales reveal ent
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::6203cf1bf32f5be48ee40e95a60caf4a
https://pubmed.ncbi.nlm.nih.gov/21922630
https://pubmed.ncbi.nlm.nih.gov/21922630
Autor:
Jeremy C. Smith, John D. Chodera, Frank Noé, Sören Doose, Markus Sauer, Marc Löllmann, Isabella Daidone
There is a gap between kinetic experiment and simulation in their views of the dynamics of complex biomolecular systems. Whereas experiments typically reveal only a few readily discernible exponential relaxations, simulations often indicate complex m
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::572d7308b3465ae23c08f3596a7b2f8a
http://hdl.handle.net/11697/20012
http://hdl.handle.net/11697/20012
Dimer formation of organic fluorophores reports on biomolecular dynamics under denaturing conditions
Stacking interactions between organic fluorophores can cause formation of non-fluorescent H-dimers. Dimer formation and dissociation of two fluorophores site-specifically incorporated in a biomolecule result in fluorescence intermittency that can rep
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a84d1a62d31139f3448bb01b3edc4c1a
https://doi.org/10.1039/c1cp21111k
https://doi.org/10.1039/c1cp21111k
Proteins have evolved to fold and function within a cellular environment that is characterized by high macromolecular content. The earliest step of protein folding represents intrachain contact formation of amino acid residues within an unfolded poly
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d89a77f9f0e6af348f4b9b2a3186a6f9
https://pub.uni-bielefeld.de/record/1596078
https://pub.uni-bielefeld.de/record/1596078
Autor:
Norbert Sewald, Sören Doose, Carolin Plattner, Marc Löllmann, Anne Burgert, Stefan Bollmann, Markus Sauer, Lilly Nagel
Publikováno v:
ResearcherID
Glycosylation of proteins plays an important role in molecular recognition among proteins with implications for a variety of cellular processes. The large amount of glycan variants enables interactions of exquisite specificity. Glycoproteins often ar
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::97f76ce26ad86b1caf03afbb19339039
https://doi.org/10.1016/j.bpj.2011.11.076
https://doi.org/10.1016/j.bpj.2011.11.076
Publikováno v:
Biophysical Journal. 98:46a
Glycine-serine polypeptides in aqueous solution behave as unstructured polymers that exhibit end-to-end contact rates dependent on contour length and in accordance with polymer theory. Aggregation-prone peptides like polyglutamine (poly-Q, associated
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::5284a97402334c22843d34aa50558488
https://doi.org/10.1016/j.bpj.2009.12.264
https://doi.org/10.1016/j.bpj.2009.12.264