Spectral editing at ultra-fast magic-angle-spinning in solid-state NMR: facilitating protein sequential signal assignment by HIGHLIGHT approach.

about

Application of paramagnetic relaxation enhancements to accelerate the acquisition of 2D and 3D solid-state NMR spectra of oriented membrane proteins.

P2860

Q47258046-C0F83E43-D40C-42A2-8BFD-8F00E267797F

P2860

Spectral editing at ultra-fast magic-angle-spinning in solid-state NMR: facilitating protein sequential signal assignment by HIGHLIGHT approach.

Item

http://www.wikidata.org/entity/Q40092466

description

2016 nî lūn-bûn

@nan

2016年の論文

@ja

2016年論文

@yue

2016年論文

@zh-hant

2016年論文

@zh-hk

2016年論文

@zh-mo

2016年論文

@zh-tw

2016年论文

@wuu

2016年论文

@zh

2016年论文

@zh-cn

name

Spectral editing at ultra-fast ...... ignment by HIGHLIGHT approach.

@en

type

Item

label

Spectral editing at ultra-fast ...... ignment by HIGHLIGHT approach.

@en

prefLabel

Spectral editing at ultra-fast ...... ignment by HIGHLIGHT approach.

@en

P1476

Spectral editing at ultra-fast ...... signment by HIGHLIGHT approach

@en

P2093

Fei Long

http://www.w3.org/2001/XMLSchema#string

Isamu Matsuda

http://www.w3.org/2001/XMLSchema#string

Songlin Wang

http://www.w3.org/2001/XMLSchema#string

P2860

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

Resonance Assignment and Three-Dimensional Structure Determination of a Human α-Defensin, HNP-1, by Solid-State NMR

Structure of the amantadine binding site of influenza M2 proton channels in lipid bilayers

X-ray and NMR crystallography in an enzyme active site: the indoline quinonoid intermediate in tryptophan synthase

Structural topology of phospholamban pentamer in lipid bilayers by a hybrid solution and solid-state NMR method

Structure and backbone dynamics of a microcrystalline metalloprotein by solid-state NMR

A structural model for Alzheimer's beta -amyloid fibrils based on experimental constraints from solid state NMR

Orientation of the Escherichia coli outer membrane protein OmpX in phospholipid bilayer membranes determined by solid-State NMR.

Revealing protein structures in solid-phase peptide synthesis by 13C solid-state NMR: evidence of excessive misfolding for Alzheimer's β.

Combination of ¹⁵N reverse labeling and afterglow spectroscopy for assigning membrane protein spectra by magic-angle-spinning solid-state NMR: application to the multidrug resistance protein EmrE

P2888

s10858-016-0014-4

P304

131-141

http://www.w3.org/2001/XMLSchema#string

P31

scholarly article

P356

10.1007/S10858-016-0014-4

http://www.w3.org/2001/XMLSchema#string

P433

http://www.w3.org/2001/XMLSchema#string

P478

http://www.w3.org/2001/XMLSchema#string

P50

Yoshitaka Ishii

P577

2016-01-19T00:00:00Z

http://www.w3.org/2001/XMLSchema#dateTime

P6179

1015282455

http://www.w3.org/2001/XMLSchema#string

P698

26781951

http://www.w3.org/2001/XMLSchema#string

Spectral editing at ultra-fast magic-angle-spinning in solid-state NMR: facilitating protein sequential signal assignment by HIGHLIGHT approach.

about

P2860

P2860

Spectral editing at ultra-fast magic-angle-spinning in solid-state NMR: facilitating protein sequential signal assignment by HIGHLIGHT approach.

description

name

type

label

prefLabel

P1433

P1476

P2093

P2860

P2888

P304

P31

P356

P433

P478

P50

P577

P6179

P698

P356

P1433

P1476

P2093

P2860

P2888

P304

P31

P356

P433

P478

P50

P577

P6179

P698