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Bogdan Barz

Showing results (1-10 of 24) with videos related to

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Chemistry (Weinheim an Der Bergstrasse, Germany)|May 3, 2016
Understanding Amyloid-β Oligomerization at the Molecular Level: The Role of the Fibril SurfaceBogdan Barz, Birgit Strodel
Progress in Molecular Biology and Translational Science|March 9, 2020
PrefaceBirgit Strodel, Bogdan Barz
Plos One|April 18, 2012
Dimer formation enhances structural differences between amyloid β-protein (1-40) and (1-42): an explicit-solvent molecular dynamics studyBogdan Barz, Brigita Urbanc
The Journal of Physical Chemistry. B|February 28, 2014
Minimal model of self-assembly: emergence of diversity and complexityBogdan Barz, Brigita Urbanc
The Journal of Chemical Physics|February 18, 2006
Calculating potentials of mean force and diffusion coefficients from nonequilibrium processes without Jarzynski's equalityIoan Kosztin, Bogdan Barz, Lorant Janosi
Journal of the American Chemical Society|December 14, 2017
Pathways of Amyloid-β Aggregation Depend on Oligomer ShapeBogdan Barz, Qinghua Liao, Birgit Strodel
Plos Computational Biology|October 8, 2019
Large-scale, dynamin-like motions of the human guanylate binding protein 1 revealed by multi-resolution simulationsBogdan Barz, Jennifer Loschwitz, Birgit Strodel
Chemical Communications (Cambridge, England)|January 5, 2021
Compact fibril-like structure of amyloid β-peptide (1-42) monomersBogdan Barz, Alexander K Buell, Soumav Nath
Biochimica Et Biophysica Acta|January 8, 2008
Membrane curvature and surface area per lipid affect the conformation and oligomeric state of HIV-1 fusion peptide: a combined FTIR and MD simulation studyBogdan Barz, Tuck C Wong, Ioan Kosztin
Physical Chemistry Chemical Physics : PCCP|June 12, 2023
Pyroglutamate-modified amyloid β(3-42) monomer has more β-sheet content than the amyloid β(1-42) monomerSoumav Nath, Alexander K Buell, Bogdan Barz
Pageof 3

Showing results (1-10 of 24) with videos related to

Sort By:
Pageof 3
Chemistry (Weinheim an Der Bergstrasse, Germany)|May 3, 2016
Understanding Amyloid-β Oligomerization at the Molecular Level: The Role of the Fibril SurfaceBogdan Barz, Birgit Strodel
Progress in Molecular Biology and Translational Science|March 9, 2020
PrefaceBirgit Strodel, Bogdan Barz
Plos One|April 18, 2012
Dimer formation enhances structural differences between amyloid β-protein (1-40) and (1-42): an explicit-solvent molecular dynamics studyBogdan Barz, Brigita Urbanc
The Journal of Physical Chemistry. B|February 28, 2014
Minimal model of self-assembly: emergence of diversity and complexityBogdan Barz, Brigita Urbanc
The Journal of Chemical Physics|February 18, 2006
Calculating potentials of mean force and diffusion coefficients from nonequilibrium processes without Jarzynski's equalityIoan Kosztin, Bogdan Barz, Lorant Janosi
Journal of the American Chemical Society|December 14, 2017
Pathways of Amyloid-β Aggregation Depend on Oligomer ShapeBogdan Barz, Qinghua Liao, Birgit Strodel
Plos Computational Biology|October 8, 2019
Large-scale, dynamin-like motions of the human guanylate binding protein 1 revealed by multi-resolution simulationsBogdan Barz, Jennifer Loschwitz, Birgit Strodel
Chemical Communications (Cambridge, England)|January 5, 2021
Compact fibril-like structure of amyloid β-peptide (1-42) monomersBogdan Barz, Alexander K Buell, Soumav Nath
Biochimica Et Biophysica Acta|January 8, 2008
Membrane curvature and surface area per lipid affect the conformation and oligomeric state of HIV-1 fusion peptide: a combined FTIR and MD simulation studyBogdan Barz, Tuck C Wong, Ioan Kosztin
Physical Chemistry Chemical Physics : PCCP|June 12, 2023
Pyroglutamate-modified amyloid β(3-42) monomer has more β-sheet content than the amyloid β(1-42) monomerSoumav Nath, Alexander K Buell, Bogdan Barz
Pageof 3