Pages that link to "Q33763065"
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The following pages link to Site-specific backbone amide (15)N chemical shift anisotropy tensors in a small protein from liquid crystal and cross-correlated relaxation measurements (Q33763065):
Displaying 35 items.
- The complete influenza hemagglutinin fusion domain adopts a tight helical hairpin arrangement at the lipid:water interface (Q27662151) (← links)
- Ultrahigh resolution protein structures using NMR chemical shift tensors (Q27674712) (← links)
- The impact of influenza hemagglutinin fusion peptide length and viral subtype on its structure and dynamics (Q28275832) (← links)
- The Use of Residual Dipolar Coupling in Studying Proteins by NMR (Q30407518) (← links)
- Starting-structure dependence of nanosecond timescale intersubstate transitions and reproducibility of MD-derived order parameters (Q30577861) (← links)
- Structural dynamics and conformational equilibria of SERCA regulatory proteins in membranes by solid-state NMR restrained simulations. (Q33803663) (← links)
- 15N solid-state NMR as a probe of flavin H-bonding (Q33913952) (← links)
- The impact of hydrogen bonding on amide 1H chemical shift anisotropy studied by cross-correlated relaxation and liquid crystal NMR spectroscopy (Q34042376) (← links)
- A device for the measurement of residual chemical shift anisotropy and residual dipolar coupling in soluble and membrane-associated proteins (Q34139584) (← links)
- Facile measurement of 1H–15N residual dipolar couplings in larger perdeuterated proteins (Q34180079) (← links)
- Structural NMR of protein oligomers using hybrid methods (Q34579372) (← links)
- Structural plasticity in human heterochromatin protein 1β (Q34667860) (← links)
- (15)N CSA tensors and (15)N-(1)H dipolar couplings of protein hydrophobic core residues investigated by static solid-state NMR. (Q36144628) (← links)
- Nucleophosmin integrates within the nucleolus via multi-modal interactions with proteins displaying R-rich linear motifs and rRNA. (Q36673676) (← links)
- Proton-detected 3D (15)N/(1)H/(1)H isotropic/anisotropic/isotropic chemical shift correlation solid-state NMR at 70kHz MAS. (Q36995442) (← links)
- Dynamics of biomolecules from picoseconds to seconds at atomic resolution (Q37917268) (← links)
- NMR studies of dynamic biomolecular conformational ensembles (Q38351227) (← links)
- Calculation of chemical shift anisotropy in proteins (Q38742258) (← links)
- Quantifying protein dynamics in the ps-ns time regime by NMR relaxation (Q39297293) (← links)
- Coupled motion in proteins revealed by pressure perturbation (Q41858684) (← links)
- A 13C labeling strategy reveals a range of aromatic side chain motion in calmodulin (Q42116205) (← links)
- Quantum chemical calculations of amide-15N chemical shift anisotropy tensors for a membrane-bound cytochrome-b5. (Q42137311) (← links)
- Determination of 15N chemical shift anisotropy from a membrane-bound protein by NMR spectroscopy (Q42211095) (← links)
- Very large residual dipolar couplings from deuterated ubiquitin (Q42660425) (← links)
- Time-shared experiments for efficient assignment of triple-selectively labeled proteins (Q42695740) (← links)
- Density functional calculations of backbone 15N shielding tensors in beta-sheet and turn residues of protein G. (Q42725118) (← links)
- Influence of the O-phosphorylation of serine, threonine and tyrosine in proteins on the amidic ¹⁵N chemical shielding anisotropy tensors (Q43938393) (← links)
- Improved accuracy in measuring one-bond and two-bond (15)N, (13)C (α) coupling constants in proteins by double-inphase/antiphase (DIPAP) spectroscopy (Q44579062) (← links)
- Motion of a Disordered Polypeptide Chain as Studied by Paramagnetic Relaxation Enhancements,15N Relaxation, and Molecular Dynamics Simulations: How Fast Is Segmental Diffusion in Denatured Ubiquitin? (Q51606664) (← links)
- Fast evaluation of protein dynamics from deficient 15N relaxation data. (Q55008513) (← links)
- Recovering lost magnetization: polarization enhancement in biomolecular NMR (Q83053299) (← links)
- Spectral density mapping protocols for analysis of molecular motions in disordered proteins (Q87269644) (← links)
- Extensive tests and evaluation of the CHARMM36IDPSFF force field for intrinsically disordered proteins and folded proteins (Q90273196) (← links)
- What Drives 15N Spin Relaxation in Disordered Proteins? Combined NMR/MD Study of the H4 Histone Tail (Q90346190) (← links)
- Residue-Specific Force Field Improving the Sample of Intrinsically Disordered Proteins and Folded Proteins (Q90715216) (← links)