Zobrazeno 1 - 10
of 42
pro vyhledávání: '"Janković, Brankica"'
MCL-1 and its natural inhibitors, the BH3-only proteins PUMA, BIM, and NOXA regulate apoptosis by interacting promiscuously within an entangled binding network. Little is known about the transient processes and dynamic conformational fluctuations tha
Externí odkaz:
http://arxiv.org/abs/2211.08934
Controlling the activity of proteins with azobenzene photoswitches is a potent tool for manipulating their biological function. With the help of light, one can change e.g. binding affinities, control allostery or temper with complex biological proces
Externí odkaz:
http://arxiv.org/abs/2106.06289
Autor:
Jankovic, Brankica, Ruf, Jeannette, Zanobini, Claudio, Bozovic, Olga, Buhrke, David, Hamm, Peter
The photo-triggered unbinding of the intrinsically disordered S-peptide from the RNase S complex is studied with the help of transient IR spectroscopy, covering a wide range of time scales from 100 ps to 10 ms. To that end, an azobenzene moiety has b
Externí odkaz:
http://arxiv.org/abs/2103.13053
Autor:
Bozovic, Olga, Ruf, Jeannette, Zanobini, Claudio, Jankovic, Brankica, Buhrke, David, Johnson, Philip J. M., Hamm, Peter
While much is known about different allosteric regulation mechanisms, the nature of the "allosteric signal", and the timescale on which it propagates, remains elusive. The PDZ3 domain from postsynaptic density-95 protein is a small protein domain wit
Externí odkaz:
http://arxiv.org/abs/2103.10719
The dynamics of peptide-protein binding and unbinding of a variant of the RNase S system has been investigated. To initiate the process, a photoswitchable azobenzene moiety has been covalently linked to the S-peptide, thereby switching its binding af
Externí odkaz:
http://arxiv.org/abs/2102.12925
Autor:
Bozovic, Olga, Zanobini, Claudio, Gulzar, Adnan, Jankovic, Brankica, Buhrke, David, Post, Matthias, Wolf, Steffen, Stock, Gerhard, Hamm, Peter
Publikováno v:
Proc. Natl. Acad. Sci. USA 117, 26031-26039 (2020)
While allostery is of paramount importance for protein regulation, the underlying dynamical process of ligand (un)binding at one site, resulting time evolution of the protein structure, and change of the binding affinity at a remote site is not well
Externí odkaz:
http://arxiv.org/abs/2008.01625
Publikováno v:
In Spectrochimica Acta Part A: Molecular and Biomolecular Spectroscopy 15 March 2020 229
Publikováno v:
Journal of Chemical Physics; 3/7/2023, Vol. 158 Issue 9, p1-10, 10p
Publikováno v:
FACTA UNIVERSITATIS - Law and Politics. 17(2):101-112
Externí odkaz:
https://www.ceeol.com/search/article-detail?id=793549
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