Assigning large proteins in the solid state: a MAS NMR resonance assignment strategy using selectively and extensively 13C-labelled proteins.
about
Solid-state NMR and SAXS studies provide a structural basis for the activation of αB-crystallin oligomersN-terminal domain of B-crystallin provides a conformational switch for multimerization and structural heterogeneitySolid-state NMR spectroscopy structure determination of a lipid-embedded heptahelical membrane proteinStructure of the Dimerization Interface in the Mature HIV-1 Capsid Protein Lattice from Solid State NMR of Tubular AssembliesMembrane proteins in their native habitat as seen by solid-state NMR spectroscopyHigh-Resolution NMR Studies of Human Tissue FactorLipid bilayer-bound conformation of an integral membrane beta barrel protein by multidimensional MAS NMR.Insight into the conformational stability of membrane-embedded BamA using a combined solution and solid-state NMR approach.NMR structures of polytopic integral membrane proteins.Selectively dispersed isotope labeling for protein structure determination by magic angle spinning NMR.Major Variations in HIV-1 Capsid Assembly Morphologies Involve Minor Variations in Molecular Structures of Structurally Ordered Protein Segments.In situ structural characterization of a recombinant protein in native Escherichia coli membranes with solid-state magic-angle-spinning NMR.A software framework for analysing solid-state MAS NMR data.G-protein-coupled receptor structure, ligand binding and activation as studied by solid-state NMR spectroscopy.Prediction of peak overlap in NMR spectra.Rapid prediction of multi-dimensional NMR data sets.Structural and dynamical characterization of tubular HIV-1 capsid protein assemblies by solid state nuclear magnetic resonance and electron microscopyAssignment strategies for large proteins by magic-angle spinning NMR: the 21-kDa disulfide-bond-forming enzyme DsbA.A Monte Carlo/simulated annealing algorithm for sequential resonance assignment in solid state NMR of uniformly labeled proteins with magic-angle spinning.Spin diffusion driven by R-symmetry sequences: applications to homonuclear correlation spectroscopy in MAS NMR of biological and organic solids.Structured regions of α-synuclein fibrils include the early-onset Parkinson's disease mutation sites.On the problem of resonance assignments in solid state NMR of uniformly ¹⁵N,¹³C-labeled proteins.Efficient and stable reconstitution of the ABC transporter BmrA for solid-state NMR studiesFrequency-selective heteronuclear dephasing and selective carbonyl labeling to deconvolute crowded spectra of membrane proteins by magic angle spinning NMR.High resolution structural characterization of Aβ42 amyloid fibrils by magic angle spinning NMR.Zero-quantum stochastic dipolar recoupling in solid state nuclear magnetic resonance.Isotope labeling for solution and solid-state NMR spectroscopy of membrane proteinsEfficient resonance assignment of proteins in MAS NMR by simultaneous intra- and inter-residue 3D correlation spectroscopy.Broadband homonuclear correlation spectroscopy driven by combined R2(n)(v) sequences under fast magic angle spinning for NMR structural analysis of organic and biological solids.Identifying inter-residue resonances in crowded 2D (13)C- (13)C chemical shift correlation spectra of membrane proteins by solid-state MAS NMR difference spectroscopyNMR investigation of the role of osteocalcin and osteopontin at the organic-inorganic interface in bone.Site-specific structural variations accompanying tubular assembly of the HIV-1 capsid protein.Solid-state NMR spectroscopy on complex biomolecules.Nuclear magnetic resonance (NMR) applied to membrane-protein complexes.Structural biology of supramolecular assemblies by magic-angle spinning NMR spectroscopy.Specific labeling of threonine methyl groups for NMR studies of protein-nucleic acid complexes.Secondary structure in the core of amyloid fibrils formed from human β₂m and its truncated variant ΔN6.Bacterial Filamentous Appendages Investigated by Solid-State NMR Spectroscopy.MAK33 antibody light chain amyloid fibrils are similar to oligomeric precursors.Unambiguous assignment of short- and long-range structural restraints by solid-state NMR spectroscopy with segmental isotope labeling.
P2860
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P2860
Assigning large proteins in the solid state: a MAS NMR resonance assignment strategy using selectively and extensively 13C-labelled proteins.
description
2009 nî lūn-bûn
@nan
2009 թուականի Յուլիսին հրատարակուած գիտական յօդուած
@hyw
2009 թվականի հուլիսին հրատարակված գիտական հոդված
@hy
2009年の論文
@ja
2009年論文
@yue
2009年論文
@zh-hant
2009年論文
@zh-hk
2009年論文
@zh-mo
2009年論文
@zh-tw
2009年论文
@wuu
name
Assigning large proteins in th ...... nsively 13C-labelled proteins.
@ast
Assigning large proteins in th ...... nsively 13C-labelled proteins.
@en
type
label
Assigning large proteins in th ...... nsively 13C-labelled proteins.
@ast
Assigning large proteins in th ...... nsively 13C-labelled proteins.
@en
prefLabel
Assigning large proteins in th ...... nsively 13C-labelled proteins.
@ast
Assigning large proteins in th ...... nsively 13C-labelled proteins.
@en
P2093
P50
P1476
Assigning large proteins in th ...... nsively 13C-labelled proteins.
@en
P2093
Jeremy Flinders
Matthias Hiller
Sebastian Fiedler
Stefan Markovic
P2888
P304
P356
10.1007/S10858-009-9338-7
P577
2009-07-17T00:00:00Z