Zobrazeno 1 - 8
of 8
pro vyhledávání: '"Tobias Kulschewski"'
Autor:
Tobias Kulschewski, Michael Krone, Guido Reina, Katrin Scharnowski, Thomas Ertl, Jürgen Pleiss
Publikováno v:
Computer Graphics Forum. 33:191-200
The comparison of molecular surface attributes is of interest for computer aided drug design and the analysis of biochemical simulations. Due to the non-rigid nature of molecular surfaces, partial shape matching is feasible for mapping two surfaces o
Autor:
Guido Reina, Tobias Kulschewski, Thomas Ertl, Florian Friess, Michael Krone, Katrin Scharnowski, Jürgen Pleiss, Silvia Fademrecht
Publikováno v:
IEEE transactions on visualization and computer graphics. 23(1)
We present Molecular Surface Maps, a novel, view-independent, and concise representation for molecular surfaces. It transfers the well-known world map metaphor to molecular visualization. Our application maps the complex molecular surface to a simple
Publikováno v:
Journal of biotechnology 168 (2013): 462–469. doi:10.1016/j.jbiotec.2013.10.012
info:cnr-pdr/source/autori:Kulschewski, Tobias; Sasso, Francesco; Secundo, Francesco; Lotti, Marina; Pleiss, Juergen/titolo:Molecular mechanism of deactivation of C. antarctica lipase B by methanol/doi:10.1016%2Fj.jbiotec.2013.10.012/rivista:Journal of biotechnology/anno:2013/pagina_da:462/pagina_a:469/intervallo_pagine:462–469/volume:168
info:cnr-pdr/source/autori:Kulschewski, Tobias; Sasso, Francesco; Secundo, Francesco; Lotti, Marina; Pleiss, Juergen/titolo:Molecular mechanism of deactivation of C. antarctica lipase B by methanol/doi:10.1016%2Fj.jbiotec.2013.10.012/rivista:Journal of biotechnology/anno:2013/pagina_da:462/pagina_a:469/intervallo_pagine:462–469/volume:168
The catalytic activity of Candida antarctica lipase B upon alcoholysis of a constant concentration of 15.2% vinyl acetate (vol/vol) and varying concentrations of methanol (0.7–60%) in toluene was determined experimentally by measuring the initial r
Autor:
Tobias Kulschewski, Jürgen Pleiss
Publikováno v:
Molecular Simulation. 39:754-767
A set of 13 aliphatic alcohols was modelled by molecular dynamics simulations at temperatures from 288 to 338 K using the optimised potential for liquid simulations (OPLS) united-atom force field, the OPLS all-atom force field and the OPLS all-atom f
Publikováno v:
Computer Graphics Forum. 32:331-340
We present a coordinated-view application for the analysis of molecular surface features like cavities, channels and pockets. Our tool employs object-space ambient occlusion for the detection of such features and tracks them over time. It offers time
Publikováno v:
Journal of biotechnology 214 (2015): 1–8. doi:10.1016/j.jbiotec.2015.08.023
info:cnr-pdr/source/autori:Sasso, Francesco; Kulschewski, Tobias; Secundo, Francesco; Lotti, Marina; Pleiss, Jürgen/titolo:The effect of thermodynamic properties of solvent mixtures explains the difference between methanol and ethanol in C.antarctica lipase B catalyzed alcoholysis/doi:10.1016%2Fj.jbiotec.2015.08.023/rivista:Journal of biotechnology/anno:2015/pagina_da:1/pagina_a:8/intervallo_pagine:1–8/volume:214
info:cnr-pdr/source/autori:Sasso, Francesco; Kulschewski, Tobias; Secundo, Francesco; Lotti, Marina; Pleiss, Jürgen/titolo:The effect of thermodynamic properties of solvent mixtures explains the difference between methanol and ethanol in C.antarctica lipase B catalyzed alcoholysis/doi:10.1016%2Fj.jbiotec.2015.08.023/rivista:Journal of biotechnology/anno:2015/pagina_da:1/pagina_a:8/intervallo_pagine:1–8/volume:214
Kinetic modelling, molecular modelling, and experimental determination of the initial reaction velocity of lipase-catalyzed alcoholysis were combined to study the effect of the alcohol substrate to catalytic activity. The model system consisted of me
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::04eb92683d09bf5d45870ea97ca9f623
http://www.cnr.it/prodotto/i/343111
http://www.cnr.it/prodotto/i/343111
Using molecular dynamics (MD) simulations, the density of single proteins and its temperature dependence was modelled starting from the experimentally determined protein structure and a generic, transferable force field, without the need of prior par
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d4c2632030d575f0b19551e9261a0c76
Autor:
Tobias Kulschewski, Pleiss, Jürgen
Publikováno v:
Langmuir; Sep2016, Vol. 32 Issue 35, p8960-8968, 9p