about
The molecular structure of spider dragline silk: folding and orientation of the protein backboneProtein structure determination from 13C spin-diffusion solid-state NMR spectroscopyAmyloid fibrils of the HET-s(218-289) prion form a beta solenoid with a triangular hydrophobic coreAtomic-resolution three-dimensional structure of HET-s(218-289) amyloid fibrils by solid-state NMR spectroscopyA proton-detected 4D solid-state NMR experiment for protein structure determinationThe amyloid-Congo red interface at atomic resolutionDynamics and Cleavability at the alpha-cleavage site of APP(684-726) in different lipid environmentsMechanism of inhibition of enveloped virus membrane fusion by the antiviral drug arbidolUnlike twins: an NMR comparison of two α-synuclein polymorphs featuring different toxicityOptimal degree of protonation for ¹H detection of aliphatic sites in randomly deuterated proteins as a function of the MAS frequency.Atomic-resolution structure of a disease-relevant Aβ(1-42) amyloid fibril.Accelerating proton spin diffusion in perdeuterated proteins at 100 kHz MAS.4D solid-state NMR for protein structure determination.Supercontracted spider dragline silk: a solid-state NMR study of the local structure.On the behavior of water at subfreezing temperatures in a protein crystal: evidence of higher mobility than in bulk water.Adiabatic-passage cross polarization in N-15 NMR spectroscopy of peptides weakly associated to phospholipids: determination of large RDC.Orientation and conformational preference of leucine-enkephalin at the surface of a hydrated dimyristoylphosphatidylcholine bilayer: NMR and MD simulation.Hexagonal ice in pure water and biological NMR samples.Line-Broadening in Low-Temperature Solid-State NMR Spectra of Fibrils.Polarization transfer over the water-protein interface in solids.One- and two-dimensional NMR spectroscopy with a magnetic-resonance force microscope.Characterization of different water pools in solid-state NMR protein samples.Contribution of specific residues of the β-solenoid fold to HET-s prion function, amyloid structure and stability.Probing water accessibility in HET-s(218-289) amyloid fibrils by solid-state NMR.Quantitative analysis of protein backbone dynamics in microcrystalline ubiquitin by solid-state NMR spectroscopy.Structure-based drug design identifies polythiophenes as antiprion compounds.The mechanism of toxicity in HET-S/HET-s prion incompatibility.Trapping and structural elucidation of an intermediate in the macrophomate synthase reaction pathway.Correlation of structural elements and infectivity of the HET-s prion.Dipolar truncation in magic-angle spinning NMR recoupling experiments.Structural and functional studies of the nicotinic acetylcholine receptor by solid-state NMR.Atomic-resolution three-dimensional structure of amyloid β fibrils bearing the Osaka mutation.The conformation of acetylcholine at its target site in the membrane-embedded nicotinic acetylcholine receptor.Site-resolved measurement of microsecond-to-millisecond conformational-exchange processes in proteins by solid-state NMR spectroscopyPreparation and Characterization of Stable α-Synuclein Lipoprotein ParticlesAn Efficient Procedure for Removal and Inactivation of Alpha-Synuclein Assemblies from Laboratory Materials.Structural and functional characterization of two alpha-synuclein strains.Exploring amyloid formation by a de novo design.Biological solid-state NMR at ETH Zurich.The structure of fibrils from 'misfolded' proteins.
P50
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P50
description
hulumtues
@sq
researcher
@en
wetenschapper
@nl
հետազոտող
@hy
name
Beat H Meier
@ast
Beat H Meier
@en
Beat H Meier
@es
Beat H Meier
@nl
Beat H Meier
@sl
type
label
Beat H Meier
@ast
Beat H Meier
@en
Beat H Meier
@es
Beat H Meier
@nl
Beat H Meier
@sl
altLabel
B H Meier
@en
B.H. Meier
@nl
Beat Meier
@en
Meier BH
@en
prefLabel
Beat H Meier
@ast
Beat H Meier
@en
Beat H Meier
@es
Beat H Meier
@nl
Beat H Meier
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P1053
K-4066-2016
P21
P31
P3829
P496
0000-0002-9107-4464
P569
2000-01-01T00:00:00Z