Function changing mutations in glucocorticoid receptor evolution correlate with their relevance to mode coupling

Autor: Kav, B., Ozturk, M., Kabakcioglu, A.

Nonlinear effects in protein dynamics are expected to play role in function, particularly of allosteric nature, by facilitating energy transfer between vibrational modes. A recently proposed method focusing on the non-Gaussian shape of the population

Externí odkaz: http://arxiv.org/abs/1509.05483

Evaluating Polarizable Biomembrane Simulations against Experiments.

Autor: Antila HS; Department of Theory and Bio-Systems, Max Planck Institute of Colloids and Interfaces, Potsdam 14476, Germany.; Department of Biomedicine, University of Bergen, Bergen 5020, Norway.; Computational Biology Unit, Department of Informatics, University of Bergen, Bergen 5008, Norway., Dixit S; Department of Theory and Bio-Systems, Max Planck Institute of Colloids and Interfaces, Potsdam 14476, Germany., Kav B; Institute of Biological Information Processing: Structural Biochemistry (IBI-7), Forschungszentrum Jülich, Jïulich 52428, Germany., Madsen JJ; Department of Molecular Medicine, Morsani College of Medicine, University of South Florida, Tampa, Florida 33612, United States.; Center for Global Health and Infectious Diseases Research, Global and Planetary Health, College of Public Health, University of South Florida, Tampa, Florida 33612, United States of America., Miettinen MS; Department of Theory and Bio-Systems, Max Planck Institute of Colloids and Interfaces, Potsdam 14476, Germany.; Computational Biology Unit, Department of Informatics, University of Bergen, Bergen 5008, Norway.; Department of Chemistry, University of Bergen, Bergen 5007, Norway., Ollila OHS; VTT Technical Research Centre of Finland, Espoo 02044, Finland.; Institute of Biotechnology, University of Helsinki, Helsinki 00014, Finland.

Publikováno v: Journal of chemical theory and computation [J Chem Theory Comput] 2024 May 28; Vol. 20 (10), pp. 4325-4337. Date of Electronic Publication: 2024 May 08.

NMRlipids Databank makes data-driven analysis of biomembrane properties accessible for all

Autor: Kiirikki, A., Antila, H., Bort, L., Buslaev, P., Favela, F., Ferreira, T., Fuchs, P., Garcia-Fandino, R., Gushchin, I., Kav, B., Kula, P., Kurki, M., Kuzmin, A., Madsen, J., Miettinen, M., Nencini, R., Piggot, T., Piñeiro, Á., Samantray, S., Suarez-Leston, F., Ollila, O.

Publikováno v: Research Square
ChemRxiv : the Preprint Server for Chemistry

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=dedup_wf_001::618387ccd26a2165c63385471f2878cd
https://hdl.handle.net/21.11116/0000-000D-4E5D-521.11116/0000-000D-4E5F-3

Binding and segregation of proteins in membrane adhesion: Theory, modelling, and simulations

Autor: Weikl, T., Hu, J., Kav, B., Różycki, B.

Publikováno v: Advances in Biomembranes and Lipid Self-Assembly
Multiresponsive Behavior of Biomembranes and Giant Vesicles

The adhesion of biomembranes is mediated by the binding of membrane-anchored receptor and ligand proteins. The proteins can only bind if the separation between apposing membranes is sufficiently close to the length of the protein complexes, which lea

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::422dddb3478db8366e6ca7f237f70b05
http://arxiv.org/abs/1911.09352

Probing the Link between Pancratistatin and Mitochondrial Apoptosis through Changes in the Membrane Dynamics on the Nanoscale.

Autor: Castillo SR; Department of Chemistry and Biochemistry, University of Windsor, Windsor, Ontario N9B 3P4, Canada., Rickeard BW; Department of Chemistry and Biochemistry, University of Windsor, Windsor, Ontario N9B 3P4, Canada., DiPasquale M; Department of Chemistry and Biochemistry, University of Windsor, Windsor, Ontario N9B 3P4, Canada., Nguyen MHL; Department of Chemistry and Biochemistry, University of Windsor, Windsor, Ontario N9B 3P4, Canada., Lewis-Laurent A; Department of Chemistry and Biochemistry, University of Windsor, Windsor, Ontario N9B 3P4, Canada., Doktorova M; Department of Molecular Physiology and Biological Physics, University of Virginia School of Medicine, Charlottesville, Virginia 22903, United States., Kav B; Max-Planck Institute of Colloids and Interfaces, Potsdam 14476, Germany.; Institute of Biological Information Processing: Structural Biochemistry (IBI-7), Forschungszentrum Julich, Julich 52428, Germany., Miettinen MS; Max-Planck Institute of Colloids and Interfaces, Potsdam 14476, Germany., Nagao M; National Institute of Standards and Technology, Center for Neutron Research, Gaithersburg, Maryland 20899, United States.; Department of Materials Science and Engineering, University of Maryland, College Park, Maryland 20742, United States.; Department of Physics and Astronomy, University of Delaware, Newark, Delaware 19716, United States., Kelley EG; National Institute of Standards and Technology, Center for Neutron Research, Gaithersburg, Maryland 20899, United States., Marquardt D; Department of Chemistry and Biochemistry, University of Windsor, Windsor, Ontario N9B 3P4, Canada.; Department of Physics, University of Windsor, Windsor, Ontario N9B 3P4, Canada.

Publikováno v: Molecular pharmaceutics [Mol Pharm] 2022 Jun 06; Vol. 19 (6), pp. 1839-1852. Date of Electronic Publication: 2022 May 13.