Translational diffusion measured by PFG-NMR on full length and fragments of the Alzheimer Aβ(1-40) peptide. Determination of hydrodynamic radii of random coil peptides of varying length
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Structural features of proinsulin C-peptide oligomeric and amyloid statesCutting off functional loops from homodimeric enzyme superoxide dismutase 1 (SOD1) leaves monomeric β-barrels.Energy landscapes of the monomer and dimer of the Alzheimer's peptide Abeta(1-28).Tetracycline prevents Aβ oligomer toxicity through an atypical supramolecular interaction.Viscous friction between crystalline and amorphous phase of dragline silk.Zinc as chaperone-mimicking agent for retardation of amyloid β peptide fibril formation.The hairpin conformation of the amyloid β peptide is an important structural motif along the aggregation pathway.Misfolding of amyloidogenic proteins and their interactions with membranes.Intrinsic α helix propensities compact hydrodynamic radii in intrinsically disordered proteins.Identification of small-molecule binding pockets in the soluble monomeric form of the Aβ42 peptide.Solution NMR studies of recombinant Aβ(1-42): from the presence of a micellar entity to residual β-sheet structure in the soluble species.pH-Dependent Interaction between C-Peptide and Phospholipid BicellesPhotochemical regulation of an artificial hydrolase by a backbone incorporated tertiary structure switch.Characterization of the internal dynamics and conformational space of zinc-bound amyloid β peptides by replica-exchange molecular dynamics simulations.A (4R)- or a (4S)-fluoroproline residue in position Xaa of the (Xaa-Yaa-Gly) collagen repeat severely affects triple-helix formation.Distinct conformational states of the Alzheimer β-amyloid peptide can be detected by high-pressure NMR spectroscopy.Secondary structure conversions of Alzheimer's Abeta(1-40) peptide induced by membrane-mimicking detergents.Hydrodynamic effects on β-amyloid (16-22) peptide aggregation.The influence of incorporating lipids or liposaccharides on the particle size of peptide therapeutics.Understanding Amyloid-β Oligomerization at the Molecular Level: The Role of the Fibril Surface.A left-handed 3(1) helical conformation in the Alzheimer Abeta(12-28) peptide.High-resolution NMR studies of the zinc-binding site of the Alzheimer's amyloid beta-peptide.Translational, rotational and internal dynamics of amyloid beta-peptides (Abeta40 and Abeta42) from molecular dynamics simulations.Bioinspired Reversibly Cross-linked Hydrogels Comprising Polypeptide Micelles Exhibit Enhanced Mechanical PropertiesMethods to determine slow diffusion coefficients of biomolecules. Applications to Engrailed 2, a partially disordered protein
P2860
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P2860
Translational diffusion measured by PFG-NMR on full length and fragments of the Alzheimer Aβ(1-40) peptide. Determination of hydrodynamic radii of random coil peptides of varying length
description
im November 2002 veröffentlichter wissenschaftlicher Artikel
@de
wetenschappelijk artikel
@nl
наукова стаття, опублікована в листопаді 2002
@uk
name
Translational diffusion measur ...... fragments of the Alzheimer Aβ
@nl
Translational diffusion measur ...... oil peptides of varying length
@en
type
label
Translational diffusion measur ...... fragments of the Alzheimer Aβ
@nl
Translational diffusion measur ...... oil peptides of varying length
@en
prefLabel
Translational diffusion measur ...... fragments of the Alzheimer Aβ
@nl
Translational diffusion measur ...... oil peptides of varying length
@en
P2860
P50
P356
P1476
Translational diffusion measur ...... oil peptides of varying length
@en
P2093
Peter Damberg
P2860
P304
P356
10.1002/MRC.1132
P577
2002-11-08T00:00:00Z