Zobrazeno 1 - 10
of 18
pro vyhledávání: '"Hannes G, Wallnoefer"'
Autor:
Julian E Fuchs, Susanne von Grafenstein, Roland G Huber, Michael A Margreiter, Gudrun M Spitzer, Hannes G Wallnoefer, Klaus R Liedl
Publikováno v:
PLoS Computational Biology, Vol 9, Iss 4, p e1003007 (2013)
A purely information theory-guided approach to quantitatively characterize protease specificity is established. We calculate an entropy value for each protease subpocket based on sequences of cleaved substrates extracted from the MEROPS database. We
Externí odkaz:
https://doaj.org/article/12762a534f704b2c91b9811464d758a5
Autor:
Julian E Fuchs, Roland G Huber, Susanne von Grafenstein, Hannes G Wallnoefer, Gudrun M Spitzer, Dietmar Fuchs, Klaus R Liedl
Publikováno v:
PLoS ONE, Vol 7, Iss 12, p e53005 (2012)
Recent clinical studies revealed increased phenylalanine levels and phenylalanine to tyrosine ratios in patients suffering from infection, inflammation and general immune activity. These data implicated down-regulation of activity of phenylalanine hy
Externí odkaz:
https://doaj.org/article/80c6d4828a3a411d9bdf3363f15e75a6
Publikováno v:
Journal of Computational Chemistry. 32:1743-1752
Factor Xa (fXa) is a promising target for antithrombotic drugs. Recently, we presented a molecular dynamics study on fXa, which highlighted the need for a careful system setup to obtain stable simulations. Here, we show that these simulations can be
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::0ebec56a4e3f995fe2af44176514dbc4
https://doi.org/10.1002/jcc.21758
https://doi.org/10.1002/jcc.21758
Publikováno v:
Journal of the America Chemical Society; Volumen 132, Número 30. 2010
Kérwá
Universidad de Costa Rica
instacron:UCR
Kérwá
Universidad de Costa Rica
instacron:UCR
Protein-protein interfaces have crucial functions in many biological processes. The large interaction areas of such interfaces show complex interaction motifs. Even more challenging is the understanding of (multi)specificity in protein-protein bindin
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::caa5847612d0ede07936b0709669d37f
https://doi.org/10.1021/ja909908y
https://doi.org/10.1021/ja909908y
Publikováno v:
The Journal of Physical Chemistry B. 114:7405-7412
The role of water molecules is increasingly attracting attention in structural biology, and many studies have demonstrated their crucial contribution to the stability and function of proteins. Here, we present molecular dynamics studies on factor Xa
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::8fb4901f4bd5e69d2e66ec666a9db76f
https://doi.org/10.1021/jp101654g
https://doi.org/10.1021/jp101654g
Autor:
Stephen J. Fox, Christofer S. Tautermann, Chris-Kriton Skylaris, Thomas R. Fox, Hannes G. Wallnoefer
Publikováno v:
Journal of chemical theory and computation. 7(4)
The accurate prediction of ligand binding affinities to a protein remains a desirable goal of computational biochemistry. Many available methods use molecular mechanics (MM) to describe the system, however, MM force fields cannot fully describe the c
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::12eb8d48044739e2fdc86aecdaac6e37
https://pubmed.ncbi.nlm.nih.gov/26606358
https://pubmed.ncbi.nlm.nih.gov/26606358
Autor:
Roland G, Huber, Julian E, Fuchs, Susanne, von Grafenstein, Monika, Laner, Hannes G, Wallnoefer, Nejma, Abdelkader, Romano T, Kroemer, Klaus R, Liedl
Publikováno v:
The Journal of Physical Chemistry. B
Entropy is an important energetic quantity determining the progression of chemical processes. We propose a new approach to obtain hydration entropy directly from probability density functions in state space. We demonstrate the validity of our approac
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::906b6a3b5c3f65ce8a2d10154379d40c
https://pubmed.ncbi.nlm.nih.gov/23651109
https://pubmed.ncbi.nlm.nih.gov/23651109
Autor:
Julian E, Fuchs, Susanne, von Grafenstein, Roland G, Huber, Michael A, Margreiter, Gudrun M, Spitzer, Hannes G, Wallnoefer, Klaus R, Liedl
Publikováno v:
PLoS Computational Biology
A purely information theory-guided approach to quantitatively characterize protease specificity is established. We calculate an entropy value for each protease subpocket based on sequences of cleaved substrates extracted from the MEROPS database. We
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::fbc07977be41f46e2bfd2736ef459e0e
https://pubmed.ncbi.nlm.nih.gov/23637583
https://pubmed.ncbi.nlm.nih.gov/23637583
Publikováno v:
Journal of chemical information and modeling. 51(11)
Structural water molecules are crucial for the stability and function of proteins. Recently, we presented a molecular dynamics (MD) study on blood coagulation factor Xa (fXa) to investigate the effect of water molecules on the flexibility of the prot
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::07703402e0336e5152f2be8632671216
https://pubmed.ncbi.nlm.nih.gov/21970362
https://pubmed.ncbi.nlm.nih.gov/21970362
Publikováno v:
Challenges and Advances in Computational Chemistry and Physics ISBN: 9789048130337
Many computational methods have become standard techniques in modern drug discovery. However, approaches which employ explicit molecular dynamics simulations still are restricted to special applications, as their extensive computational requirements
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::0a3f17693585298d1af3efb6fb03e689
https://doi.org/10.1007/978-90-481-3034-4_16
https://doi.org/10.1007/978-90-481-3034-4_16
