about
11th German Conference on Chemoinformatics (GCC 2015) : Fulda, Germany. 8-10 November 2015.β-sheet propensity controls the kinetic pathways and morphologies of seeded peptide aggregation.Effects of surface interactions on peptide aggregate morphology.Effect of beta-sheet propensity on peptide aggregation.The effect of surface tethering on the folding of the src-SH3 protein domain.Stability of a protein tethered to a surface.Effects of surface tethering on protein folding mechanisms.Effects of frustration, confinement, and surface interactions on the dimerization of an off-lattice beta-barrel protein.Reconstruction of the src-SH3 protein domain transition state ensemble using multiscale molecular dynamics simulations.Self-assembly of peptides into a beta-barrel motif.Temperature dependence of the free energy landscape of the src-SH3 protein domain.Posttransition state desolvation of the hydrophobic core of the src-SH3 protein domainProbing the folding free energy landscape of the Src-SH3 protein domain.Sequence periodicity and secondary structure propensity in model proteins.Human islet amyloid polypeptide monomers form ordered beta-hairpins: a possible direct amyloidogenic precursor.Amyloid β-Protein C-Terminal Fragments: Formation of Cylindrins and β-Barrels.Folding of the 25 residue Abeta(12-36) peptide in TFE/water: temperature-dependent transition from a funneled free-energy landscape to a rugged one.
P50
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P50
description
hulumtuese
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onderzoeker
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հետազոտող
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Joan-Emma Shea
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Joan-Emma Shea
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Joan-Emma Shea
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Joan-Emma Shea
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Joan-Emma Shea
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Joan-Emma Shea
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Joan-Emma Shea
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Joan-Emma Shea
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Joan-Emma Shea
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Joan-Emma Shea
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