Zobrazeno 1 - 10
of 16
pro vyhledávání: '"Toni, Hoffmann"'
Autor:
Lorna Dougan, Toni Hoffmann, David J. Brockwell, Matthew Batchelor, Katarzyna M. Tych, Michael C. Wilson, Emanuele Paci
Publikováno v:
Soft Matter. 12:2688-2699
Proteins from extremophilic organisms provide excellent model systems to determine the role of non-covalent interactions in defining protein stability and dynamics as well as being attractive targets for the development of robust biomaterials. Hypert
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::5ec1778049b0ef19e61d2262b80541e6
https://doi.org/10.1039/c5sm02938d
https://doi.org/10.1039/c5sm02938d
Autor:
David J. Brockwell, Megan L. Hughes, Katherine E. Kendrick, Toni Hoffmann, Michael Wilson, Lorna Dougan, Danielle L. Walsh, Katarzyna M. Tych, Matthew Batchelor
Publikováno v:
Biochemical Society Transactions. 43:179-185
Extremophiles are organisms which survive and thrive in extreme environments. The proteins from extremophilic single-celled organisms have received considerable attention as they are structurally stable and functionally active under extreme physical
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::9357b35af9fd839bfcd67b9f4f66ef6e
https://doi.org/10.1042/bst20140274
https://doi.org/10.1042/bst20140274
Autor:
Michael C. Wilson, Emanuele Paci, Toni Hoffmann, Lorna Dougan, Katarzyna M. Tych, Megan L. Hughes, Matthew Batchelor, David J. Brockwell
Proteins from organisms that have adapted to environmental extremes provide attractive systems to explore and determine the origins of protein stability. Improved hydrophobic core packing and decreased loop-length flexibility can increase the thermod
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::9024b30f76f2a29575fc148175736109
http://hdl.handle.net/11585/885043
http://hdl.handle.net/11585/885043
Autor:
Jason J. Davis, Paul Ko Ferrigno, Anthony T. Buxton, Qifeng Song, Lukas K. J. Stadler, Toni Hoffmann, Simon D. Wagner, Michael Busby
Publikováno v:
Protein Engineering, Design and Selection
Non-antibody scaffold proteins are used for a range of applications, especially the assessment of protein-protein interactions within human cells. The search for a versatile, robust and biologically neutral scaffold previously led us to design STM (s
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::8cbae78d2dae9dc827507135dbab8945
https://doi.org/10.1093/protein/gzq012
https://doi.org/10.1093/protein/gzq012
Autor:
Thomas Crosskey, Bob Schiffrin, Katarzyna M. Tych, Toni Hoffmann, David J. Brockwell, Lorna Dougan
Publikováno v:
ACS nano. 9(9)
Single-molecule force spectroscopy by atomic force microscopy exploits the use of multimeric protein constructs, namely, polyproteins, to decrease the impact of nonspecific interactions, to improve data accumulation, and to allow the accommodation of
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c91f500e1070f247ece942df3569e073
https://pubmed.ncbi.nlm.nih.gov/26284289
https://pubmed.ncbi.nlm.nih.gov/26284289
Publikováno v:
Microbial Physiology. 11:82-93
Cupriavidus (Wautersia, Ralstonia, Alcaligenes) metallidurans strain CH34is a well-studied example of a metal-resistant proteobacterium. Genome sequence analysis revealed the presence of a variety of paralogs of proteins that were previously shown to
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::309417fae22d6a9ce3b48478b435df3b
https://doi.org/10.1159/000092820
https://doi.org/10.1159/000092820
Autor:
Susann Lucke, Dietrich H. Nies, Antje Legatzki, Andreas Anton, Toni Hoffmann, Sylvia Franke, Dieter Neumann
Publikováno v:
Biodegradation. 14:153-168
Quantitative models were derived to explain heavy metal resistance in Ralstonia metallidurans. A ΔczcA deletion of the gene for the central component of the Co2+/Zn2+/Cd2+ efflux system CzcCBA combined with the expression level of czcCBA as studied
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::b631af4741e205c03ae6e8127ccb1af2
https://doi.org/10.1023/a:1024043306888
https://doi.org/10.1023/a:1024043306888
Publikováno v:
Physical Chemistry Chemical Physics
The successful integration of proteins into bionanomaterials with specific and desired functions requires an accurate understanding of their material properties. Two such important properties are their mechanical stability and malleability. While sin
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c1673ce6312a8e7cf2694ddd2ee4f309
https://pubmed.ncbi.nlm.nih.gov/23989058
https://pubmed.ncbi.nlm.nih.gov/23989058
Publikováno v:
The Journal of Physical Chemistry B
Single-molecule force spectroscopy has emerged as a powerful approach to examine the stability and dynamics of single proteins. We have completed force extension experiments on the small cold shock protein B from Thermotoga maritima, using a speciall
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::4fc172ef1bf12e14965390ecb732555d
Autor:
Toni Hoffmann, Lorna Dougan
Publikováno v:
ChemInform. 43
In recent years single molecule force spectroscopy has emerged as a powerful new tool to explore the mechanical stability and folding pathways of individual proteins. This technique is used to apply a stretching force between two points of a protein,
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::0041e008a513d97b8af05a261e1939fb
https://doi.org/10.1002/chin.201241280
https://doi.org/10.1002/chin.201241280