Characterizing the assembly of the Sup35 yeast prion fragment, GNNQQNY: structural changes accompany a fiber-to-crystal switch.
about
Probing small molecule binding to amyloid fibrils.Structural characterization of GNNQQNY amyloid fibrils by magic angle spinning NMRIn Sup35p filaments (the [PSI+] prion), the globular C-terminal domains are widely offset from the amyloid fibril backboneWildtype and A30P mutant alpha-synuclein form different fibril structures.Systematic examination of polymorphism in amyloid fibrils by molecular-dynamics simulation.Interplay of sequence, topology and termini charge in determining the stability of the aggregates of GNNQQNY mutants: a molecular dynamics study.Structural complexity of a composite amyloid fibril.Structural determinants in a library of low molecular weight gelators.The physical chemistry of the amyloid phenomenon: thermodynamics and kinetics of filamentous protein aggregation.Linear dichroism as a probe of molecular structure and interactions.The architecture of amyloid-like peptide fibrils revealed by X-ray scattering, diffraction and electron microscopy.Structural and mechanical properties of TTR105-115 amyloid fibrils from compression experiments.A role for the proteasome in the turnover of Sup35p and in [PSI(+) ] prion propagation.Exploring the sequence-structure relationship for amyloid peptides.Peptides organized as bilayer membranes.Competition between crystal and fibril formation in molecular mutations of amyloidogenic peptides.Fluorescence detected linear dichroism spectroscopy: A selective and sensitive probe for fluorophores in flow-oriented systems.Energetics Underlying Twist Polymorphisms in Amyloid Fibrils.Determination of orientations of aromatic groups in self-assembled peptide fibrils by polarised Raman spectroscopy.The diversity and utility of amyloid fibrils formed by short amyloidogenic peptides.The amyloid architecture provides a scaffold for enzyme-like catalysts.Is photocleavage of DNA by YOYO-1 using a synchrotron radiation light source sequence dependent?Supramolecular amphipathicity for probing antimicrobial propensity of host defence peptides.Inhibitory effect of hydrophobic fullerenes on the β-sheet-rich oligomers of a hydrophilic GNNQQNY peptide revealed by atomistic simulationsFrom Molecular to Supramolecular Amyloid Structures: Contributions from Fiber Diffraction and Electron Microscopy
P2860
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P2860
Characterizing the assembly of the Sup35 yeast prion fragment, GNNQQNY: structural changes accompany a fiber-to-crystal switch.
description
2010 nî lūn-bûn
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2010年の論文
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2010年論文
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2010年論文
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2010年論文
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2010年論文
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name
Characterizing the assembly of ...... any a fiber-to-crystal switch.
@en
Characterizing the assembly of ...... any a fiber-to-crystal switch.
@nl
type
label
Characterizing the assembly of ...... any a fiber-to-crystal switch.
@en
Characterizing the assembly of ...... any a fiber-to-crystal switch.
@nl
prefLabel
Characterizing the assembly of ...... any a fiber-to-crystal switch.
@en
Characterizing the assembly of ...... any a fiber-to-crystal switch.
@nl
P2860
P50
P1433
P1476
Characterizing the assembly of ...... pany a fiber-to-crystal switch
@en
P2093
Karen E Marshall
Matthew R Hicks
P2860
P304
P356
10.1016/J.BPJ.2009.10.020
P407
P577
2010-01-01T00:00:00Z