Symmetry-based constant-time homonuclear dipolar recoupling in solid state NMR
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Amyloid of Rnq1p, the basis of the [PIN+] prion, has a parallel in-register beta-sheet structureMolecular structural basis for polymorphism in Alzheimer's -amyloid fibrilsAntiparallel -sheet architecture in Iowa-mutant -amyloid fibrilsMolecular Structure of β-Amyloid Fibrils in Alzheimer’s Disease Brain TissueMolecular Structure of Aggregated Amyloid-β: Insights from Solid-State Nuclear Magnetic ResonanceMolecular structure of monomorphic peptide fibrils within a kinetically trapped hydrogel networkThe Japanese Mutant Aβ (ΔE22-Aβ1−39) Forms Fibrils Instantaneously, with Low-Thioflavin T Fluorescence: Seeding of Wild-Type Aβ1−40into Atypical Fibrils by ΔE22-Aβ1−39Intermolecular structure determination of amyloid fibrils with magic-angle spinning and dynamic nuclear polarization NMR.Parallel in-register intermolecular β-sheet architectures for prion-seeded prion protein (PrP) amyloids.Prion amyloid structure explains templating: how proteins can be genes.Combining DNP NMR with segmental and specific labeling to study a yeast prion protein strain that is not parallel in-register.The core of Ure2p prion fibrils is formed by the N-terminal segment in a parallel cross-β structure: evidence from solid-state NMR.Amyloid β Protein and Alzheimer's Disease: When Computer Simulations Complement Experimental Studies.What can solid state NMR contribute to our understanding of protein folding?Evidence for novel beta-sheet structures in Iowa mutant beta-amyloid fibrils.Restraints on backbone conformations in solid state NMR studies of uniformly labeled proteins from quantitative amide 15N-15N and carbonyl 13C-13C dipolar recoupling data.Locating folds of the in-register parallel β-sheet of the Sup35p prion domain infectious amyloid.The α-helical C-terminal domain of full-length recombinant PrP converts to an in-register parallel β-sheet structure in PrP fibrils: evidence from solid state nuclear magnetic resonance.Repeat domains of melanosome matrix protein Pmel17 orthologs form amyloid fibrils at the acidic melanosomal pH.Structural evolution of Iowa mutant β-amyloid fibrils from polymorphic to homogeneous states under repeated seeded growthStructural insights into functional and pathological amyloid.Prion diseases of yeast: amyloid structure and biology.Amyloid of the Candida albicans Ure2p prion domain is infectious and has an in-register parallel β-sheet structure.Determination of relative tensor orientations by γ-encoded chemical shift anisotropy/heteronuclear dipolar coupling 3D NMR spectroscopy in biological solids.Efficient theory of dipolar recoupling in solid-state nuclear magnetic resonance of rotating solids using Floquet-Magnus expansion: application on BABA and C7 radiofrequency pulse sequences.Amyloid-like fibrils from a domain-swapping protein feature a parallel, in-register conformation without native-like interactions.Solid-state NMR studies of amyloid fibril structureSegmental polymorphism in a functional amyloid.1H-13C/1H-15N heteronuclear dipolar recoupling by R-symmetry sequences under fast magic angle spinning for dynamics analysis of biological and organic solids.Experimentally derived structural constraints for amyloid fibrils of wild-type transthyretinZero-quantum stochastic dipolar recoupling in solid state nuclear magnetic resonance.Molecular structures of amyloid and prion fibrils: consensus versus controversyPeptide conformation and supramolecular organization in amylin fibrils: constraints from solid-state NMR.Theory of stochastic dipolar recoupling in solid-state nuclear magnetic resonance.Solid-state NMR evidence for β-hairpin structure within MAX8 designer peptide nanofibers.The yin and yang of amyloid: insights from α-synuclein and repeat domain of Pmel17Seeded growth of beta-amyloid fibrils from Alzheimer's brain-derived fibrils produces a distinct fibril structure.Zero-quantum frequency-selective recoupling of homonuclear dipole-dipole interactions in solid state nuclear magnetic resonanceTwo prion variants of Sup35p have in-register parallel beta-sheet structures, independent of hydration.The functional curli amyloid is not based on in-register parallel beta-sheet structure
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P2860
Symmetry-based constant-time homonuclear dipolar recoupling in solid state NMR
description
article
@en
im Februar 2007 veröffentlichter wissenschaftlicher Artikel
@de
wetenschappelijk artikel
@nl
наукова стаття, опублікована в лютому 2007
@uk
name
Symmetry-based constant-time homonuclear dipolar recoupling in solid state NMR
@en
Symmetry-based constant-time homonuclear dipolar recoupling in solid state NMR
@nl
type
label
Symmetry-based constant-time homonuclear dipolar recoupling in solid state NMR
@en
Symmetry-based constant-time homonuclear dipolar recoupling in solid state NMR
@nl
prefLabel
Symmetry-based constant-time homonuclear dipolar recoupling in solid state NMR
@en
Symmetry-based constant-time homonuclear dipolar recoupling in solid state NMR
@nl
P2860
P356
P1476
Symmetry-based constant-time homonuclear dipolar recoupling in solid state NMR
@en
P2860
P304
P356
10.1063/1.2437194
P407
P50
P577
2007-02-14T00:00:00Z