The impact of hydrogen bonding on amide 1H chemical shift anisotropy studied by cross-correlated relaxation and liquid crystal NMR spectroscopy.
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Probabilistic validation of protein NMR chemical shift assignmentsMultidimensional magic angle spinning NMR spectroscopy for site-resolved measurement of proton chemical shift anisotropy in biological solids.Protonation, tautomerization, and rotameric structure of histidine: a comprehensive study by magic-angle-spinning solid-state NMR.Accurate measurement of heteronuclear dipolar couplings by phase-alternating R-symmetry (PARS) sequences in magic angle spinning NMR spectroscopy.Facile measurement of ¹H-¹5N residual dipolar couplings in larger perdeuterated proteinsPolyglutamine amyloid core boundaries and flanking domain dynamics in huntingtin fragment fibrils determined by solid-state nuclear magnetic resonance.A Magic-Angle Spinning NMR Method for the Site-Specific Measurement of Proton Chemical-Shift Anisotropy in Biological and Organic SolidsHsp70 biases the folding pathways of client proteins.Proton-detected 3D (15)N/(1)H/(1)H isotropic/anisotropic/isotropic chemical shift correlation solid-state NMR at 70kHz MAS.Determination of structural topology of a membrane protein in lipid bilayers using polarization optimized experiments (POE) for static and MAS solid state NMR spectroscopy.Calculation of chemical shift anisotropy in proteins.Very large residual dipolar couplings from deuterated ubiquitin.Time-shared experiments for efficient assignment of triple-selectively labeled proteins.Composite-180° pulse-based symmetry sequences to recouple proton chemical shift anisotropy tensors under ultrafast MAS solid-state NMR spectroscopy.Improved accuracy in measuring one-bond and two-bond (15)N, (13)C (α) coupling constants in proteins by double-inphase/antiphase (DIPAP) spectroscopy.1H NMR spectra part 31: 1H chemical shifts of amides in DMSO solvent.NMR of Macromolecular Assemblies and Machines at 1 GHz and Beyond: New Transformative Opportunities for Molecular Structural Biology.On the high-temperature phase of barbituric acid
P2860
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P2860
The impact of hydrogen bonding on amide 1H chemical shift anisotropy studied by cross-correlated relaxation and liquid crystal NMR spectroscopy.
description
2010 nî lūn-bûn
@nan
2010 թուականի Օգոստոսին հրատարակուած գիտական յօդուած
@hyw
2010 թվականի օգոստոսին հրատարակված գիտական հոդված
@hy
2010年の論文
@ja
2010年論文
@yue
2010年論文
@zh-hant
2010年論文
@zh-hk
2010年論文
@zh-mo
2010年論文
@zh-tw
2010年论文
@wuu
name
The impact of hydrogen bonding ...... quid crystal NMR spectroscopy.
@ast
The impact of hydrogen bonding ...... quid crystal NMR spectroscopy.
@en
The impact of hydrogen bonding ...... quid crystal NMR spectroscopy.
@nl
type
label
The impact of hydrogen bonding ...... quid crystal NMR spectroscopy.
@ast
The impact of hydrogen bonding ...... quid crystal NMR spectroscopy.
@en
The impact of hydrogen bonding ...... quid crystal NMR spectroscopy.
@nl
prefLabel
The impact of hydrogen bonding ...... quid crystal NMR spectroscopy.
@ast
The impact of hydrogen bonding ...... quid crystal NMR spectroscopy.
@en
The impact of hydrogen bonding ...... quid crystal NMR spectroscopy.
@nl
P2860
P50
P356
P1476
The impact of hydrogen bonding ...... quid crystal NMR spectroscopy.
@en
P2093
P2860
P304
10866-10875
P356
10.1021/JA103629E
P407
P577
2010-08-01T00:00:00Z