A proton-detected 4D solid-state NMR experiment for protein structure determination (Q27667130)

Sebastian Hiller

2

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Paul Schanda

Paul Schanda

3

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Beat H Meier

Beat H Meier

7

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Anja Böckmann

5

Anja Böckmann

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author name string

Matthias Huber

1

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Matthias Ernst

Amyloid fibrils of the HET-s(218-289) prion form a beta solenoid with a triangular hydrophobic core

4

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publication date

4 April 2011

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published in

ChemPhysChem

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volume

12

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issue

5

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page(s)

915-8

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cites work

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Structure of a protein determined by solid-state magic-angle-spinning NMR spectroscopy

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Solid-State Protein-Structure Determination with Proton-Detected Triple-Resonance 3D Magic-Angle-Spinning NMR Spectroscopy

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Sensitive high resolution inverse detection NMR spectroscopy of proteins in the solid state

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Attenuated T2 relaxation by mutual cancellation of dipole-dipole coupling and chemical shift anisotropy indicates an avenue to NMR structures of very large biological macromolecules in solution

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High-accuracy distance measurement between remote methyls in specifically protonated proteins.

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Theory and application of the maximum likelihood principle to NMR parameter estimation of multidimensional NMR data

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Quantification of maximum-entropy spectrum reconstructions.

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Assignments of carbon NMR resonances for microcrystalline ubiquitin

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Characterization of different water pools in solid-state NMR protein samples

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Direct detection of (3h)J(NC') hydrogen-bond scalar couplings in proteins by solid-state NMR spectroscopy

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7 January 2021

inferred from DOI database lookup

Adiabatic dipolar recoupling in solid-state NMR: the DREAM scheme

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7 January 2021

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Solid-state NMR spectroscopy of 10% 13C labeled ubiquitin: spectral simplification and stereospecific assignment of isopropyl groups

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7 January 2021

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Identifiers

DOI

10.1002/CPHC.201100062

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Fatcat ID

release_5txcnddz5jfgvoazi5q3fvpofa

1 reference

Fatcat

https://api.fatcat.wiki/v0/release/5txcnddz5jfgvoazi5q3fvpofa

24 November 2022