Zobrazeno 1 - 10
of 56
pro vyhledávání: '"Bernd W. Koenig"'
Autor:
Doreen Niether, Mona Sarter, Bernd W. Koenig, Jörg Fitter, Andreas M. Stadler, Simone Wiegand
Publikováno v:
Polymers, Vol 12, Iss 2, p 376 (2020)
Thermophoretic behavior of a free protein changes upon ligand binding and gives access to information on the binding constants. The Soret effect has also been proven to be a promising tool to gain information on the hydration layer, as the temperatur
Externí odkaz:
https://doaj.org/article/8bc5af52705646e7907da90eca3ab54e
Autor:
Yu-Fu Hung, Melanie Schwarten, Silke Hoffmann, Dieter Willbold, Ella H. Sklan, Bernd W. Koenig
Publikováno v:
Viruses, Vol 7, Iss 7, Pp 4119-4130 (2015)
Dengue virus (DENV) is an important human pathogen causing millions of disease cases and thousands of deaths worldwide. Non-structural protein 4A (NS4A) is a vital component of the viral replication complex (RC) and plays a major role in the formatio
Externí odkaz:
https://doaj.org/article/3f4b498c9d7c4082bdcd6142ee3131cd
Autor:
Victoria Steffen, Julia Otten, Susann Engelmann, Andreas Radek, Michael Limberg, Bernd W. Koenig, Stephan Noack, Wolfgang Wiechert, Martina Pohl
Publikováno v:
Sensors, Vol 16, Iss 10, p 1604 (2016)
Background: The fast development of microbial production strains for basic and fine chemicals is increasingly carried out in small scale cultivation systems to allow for higher throughput. Such parallelized systems create a need for new rapid online
Externí odkaz:
https://doaj.org/article/4f5409efc5d1424b80fc562a14855577
Autor:
Simone Wiegand, Mona Sarter, Bernd W. Koenig, Doreen Niether, Michaela Zamponi, Joerg Fitter, Andreas M. Stadler, Wiebke Lohstroh, Niina Jalarvo
Publikováno v:
The journal of physical chemistry / B 124(2), 324-335 (2020). doi:10.1021/acs.jpcb.9b08467
Molecular dynamics plays an important role for the biological function of proteins. For protein ligand interactions, changes of conformational entropy of protein and hydration layer are relevant for the binding process. Quasielastic neutron scatterin
Autor:
Jörg Stellbrink, Bernd W. Koenig, Mikko Linnolahti, Nicole Lühmann, Dieter Richter, Aizhen Niu, Reiner Zorn, Jürgen Allgaier, Isabelle Grillo, Sabine Willbold, Lewis J. Fetters
Publikováno v:
Macromolecules. 49:5397-5406
An in situ 1H NMR study has been carried out to examine the anionic initiation mechanism of 1,3-butadiene and tert-butyllithium (t-BuLi) using n-heptane as solvent. Additionally, mixtures of model compounds have been investigated ex situ to simulate
Autor:
Carsten Münk, Dieter Häussinger, Bernd W. Koenig, Dieter Willbold, Henning Hofmann, Ananda Ayyappan Jaguva Vasudevan
Publikováno v:
Journal of molecular biology. 429(8)
The retroviral restriction factors of the APOBEC3 (A3) cytidine deaminase family catalyze the deamination of cytidines in single-stranded viral DNA. APOBEC3C (A3C) is a strong antiviral factor against viral infectivity factor (vif)-deficient simian i
Autor:
Michaela Zamponi, Bernd W. Koenig, Simon Wiegand, Andreas M. Stadler, Mona Sarter, Joerg Fitter, Doreen Niether, Lohstroh Wiebke
Publikováno v:
Biophysical Journal. 116:151a
Autor:
Dieter Häussinger, Ananda Ayyappan Jaguva Vasudevan, Carsten Münk, Astrid Höppner, Sander H. J. Smits, Bernd W. Koenig
Publikováno v:
Biological chemistry 394(11), 1357-1370 (2013). doi:10.1515/hsz-2013-0165
The APOBEC3 (A3) family of cytidine deaminases plays a vital role for innate defense against retroviruses. Lentiviruses such as HIV-1 evolved the Vif protein that triggers A3 protein degradation. There are seven A3 proteins, A3A-A3H, found in humans.
Publikováno v:
Analytical Biochemistry. 408:46-52
Nanodiscs are small-sized and flat model membranes that provide a close to native environment for reconstitution of integral membrane proteins. Incorporation of membrane proteins into nanodiscs results in water-soluble proteolipid particles making th
Autor:
Rudolf Hartmann, Oliver P. Ernst, Matthias Stoldt, Joachim Granzin, Peter Henklein, Bernd W. Koenig, Dieter Willbold, Martin Heck, Sophie Feuerstein, Alexander Pulvermüller
Publikováno v:
Biochemistry. 48:10733-10742
Binding of arrestin to photoactivated phosphorylated rhodopsin terminates the amplification of visual signals in photoreceptor cells. Currently, there is no crystal structure of a rhodopsin-arrestin complex available, although structures of unbound r