Zobrazeno 1 - 10
of 21
pro vyhledávání: '"Johannes Kraml"'
Publikováno v:
Frontiers in Molecular Biosciences, Vol 7 (2021)
Susceptibility to endosomal degradation is a decisive contribution to a protein's immunogenicity. It is assumed that the processing kinetics of structured proteins are inherently linked to their probability of local unfolding. In this study, we quant
Externí odkaz:
https://doaj.org/article/88b9ab9f473f4d2b831cc23ed3a9773a
Autor:
Monica L. Fernández-Quintero, Johannes R. Loeffler, Johannes Kraml, Ursula Kahler, Anna S. Kamenik, Klaus R. Liedl
Publikováno v:
Frontiers in Immunology, Vol 9 (2019)
We present an approach to assess antibody CDR-H3 loops according to their dynamic properties using molecular dynamics simulations. We selected six antibodies in three pairs differing substantially in their individual promiscuity respectively specific
Externí odkaz:
https://doaj.org/article/a71b23e3d4964b6b85d5ad88d325485f
Autor:
Leon Sulfierry Corrêa Costa, Diego César Batista Mariano, Rafael Eduardo Oliveira Rocha, Johannes Kraml, Carlos Henrique da Silveira, Klaus Roman Liedl, Raquel Cardoso de Melo-Minardi, Leonardo Henrique Franca de Lima
Publikováno v:
Molecules, Vol 24, Iss 18, p 3215 (2019)
β-Glucosidases are enzymes with high importance for many industrial processes, catalyzing the last and limiting step of the conversion of lignocellulosic material into fermentable sugars for biofuel production. However, β-glucosidases are inhibited
Externí odkaz:
https://doaj.org/article/c1c60d6da29f406692ad56ee21fd3fd7
Autor:
Franz Waibl, Johannes Kraml, Valentin J. Hoerschinger, Florian Hofer, Anna S. Kamenik, Monica L. Fernández-Quintero, Klaus R. Liedl
Publikováno v:
The Journal of chemical physics. 156(20)
Grid Inhomogeneous Solvation Theory (GIST) has proven useful to calculate localized thermodynamic properties of water around a solute. Numerous studies have leveraged this information to enhance structure-based binding predictions. We have recently e
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::493f5911b95c19ea2823b23040ba6d80
https://pubmed.ncbi.nlm.nih.gov/35649837
https://pubmed.ncbi.nlm.nih.gov/35649837
Autor:
Monica L. Fernández-Quintero, Florian Hofer, Anna S. Kamenik, Johannes Kraml, Franz Waibl, Klaus R. Liedl, Guy Georges, Hubert Kettenberger
Publikováno v:
Biophysical Journal
A major challenge in the development of antibody biotherapeutics is their tendency to aggregate. One root cause for aggregation is exposure of hydrophobic surface regions to the solvent. Many current techniques predict the relative aggregation propen
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::5068bc0543b5b38bff10134cb8fb4397
http://europepmc.org/articles/PMC7820740
http://europepmc.org/articles/PMC7820740
Autor:
Michael Schauperl, Anna S. Kamenik, Ursula Kahler, Franz Waibl, Florian Hofer, Johannes Kraml, Klaus R. Liedl
Publikováno v:
Journal of Chemical Information and Modeling
Reliable information on partition coefficients plays a key role in drug development, as solubility decisively affects bioavailability. In a physicochemical context, the partition coefficient of a solute between two different solvents can be described
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::25168681fea25ad2563c67676a0fcca8
https://doi.org/10.1021/acs.jcim.0c00289
https://doi.org/10.1021/acs.jcim.0c00289
Publikováno v:
Journal of Chemical Theory and Computation
For more than half a century computer simulations were developed and employed to study ensemble properties of a wide variety of atomic and molecular systems with tremendous success. Nowadays, a selection of force-fields is available that describe the
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::80250b31726968d3f1d1b4e910c02922
https://doi.org/10.1021/acs.jctc.0c00204
https://doi.org/10.1021/acs.jctc.0c00204
Publikováno v:
Journal of Chemical Information and Modeling. 60:3030-3042
Enzymatic function and activity of proteases is closely controlled by the pH value. The protonation states of titratable residues in the active site react to changes in the pH value, according to t...
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::630bc415c5ba91e812d664fad9c0d138
https://doi.org/10.1021/acs.jcim.0c00190
https://doi.org/10.1021/acs.jcim.0c00190
Publikováno v:
Journal of Biomolecular Structure and Dynamics. 39:953-959
During biological events, the water molecules associated with the protein are re-oriented to adapt to the new conditions, inducing changes in the system's free energy. The characterization of water structure and thermodynamics may facilitate the pred
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::1a6dad26c0fe4b2c0c074a769d088d60
https://doi.org/10.1080/07391102.2020.1733665
https://doi.org/10.1080/07391102.2020.1733665
Autor:
Franz Waibl, Johannes Kraml, Monica L. Fernández-Quintero, Johannes R. Loeffler, Klaus R. Liedl
Publikováno v:
Journal of computer-aided molecular design. 36(2)
Hydration thermodynamics play a fundamental role in fields ranging from the pharmaceutical industry to environmental research. Numerous methods exist to predict solvation thermodynamics of compounds ranging from small molecules to large biomolecules.
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::4195cb150a49f063a0f2abc9ef140ea4
https://pubmed.ncbi.nlm.nih.gov/35031880
https://pubmed.ncbi.nlm.nih.gov/35031880