Probing protein structure by solvent perturbation of nuclear magnetic resonance spectra. Nuclear magnetic resonance spectral editing and topological mapping in proteins by paramagnetic relaxation filtering.

Probing protein structure by solvent perturbation of nuclear magnetic resonance spectra. Nuclear magnetic resonance spectral editing and topological mapping in proteins by paramagnetic relaxation filtering.

Item
http://www.wikidata.org/entity/Q30333666
Determining the orientation and localization of membrane-bound peptidesProbing the surface of a sweet protein: NMR study of MNEI with a paramagnetic probeDetermination of membrane immersion depth with O(2): a high-pressure (19)F NMR study.Mapping oxygen accessibility to ribonuclease a using high-resolution NMR relaxation spectroscopyProbing protein structure by solvent perturbation of NMR spectra: the surface accessibility of bovine pancreatic trypsin inhibitorSpin-diffusion couples proton relaxation rates for proteins in exchange with a membrane interfaceDetermining the depth of insertion of dynamically invisible membrane peptides by gel-phase ¹H spin diffusion heteronuclear correlation NMR.Solid-state NMR investigation of the depth of insertion of protegrin-1 in lipid bilayers using paramagnetic Mn2+.The native state of apomyoglobin described by proton NMR spectroscopy: interaction with the paramagnetic probe HyTEMPO and the fluorescent dye ANSRevealing an outward-facing open conformational state in a CLC Cl(-)/H(+) exchange transporterMonitoring the interaction between β2-microglobulin and the molecular chaperone αB-crystallin by NMR and mass spectrometry: αB-crystallin dissociates β2-microglobulin oligomers.NMR analysis of [methyl-13C]methionine UvrB from Bacillus caldotenax reveals UvrB-domain 4 heterodimer formation in solutionStudying the structure and dynamics of biomolecules by using soluble paramagnetic probesInterdomain flexibility in full-length matrix metalloproteinase-1 (MMP-1).Surface exposure of the methionine side chains of calmodulin in solution. A nitroxide spin label and two-dimensional NMR study.NMR-based structural biology enhanced by dynamic nuclear polarization at high magnetic field
P2860

Probing protein structure by solvent perturbation of nuclear magnetic resonance spectra. Nuclear magnetic resonance spectral editing and topological mapping in proteins by paramagnetic relaxation filtering.

Item
http://www.wikidata.org/entity/Q30333666
description
1992 nî lūn-bûn
@nan
1992 թուականի Ապրիլին հրատարակուած գիտական յօդուած
@hyw
1992 թվականի ապրիլին հրատարակված գիտական հոդված
@hy
1992年の論文
@ja
1992年論文
@yue
1992年論文
@zh-hant
1992年論文
@zh-hk
1992年論文
@zh-mo
1992年論文
@zh-tw
1992年论文
@wuu
name
Probing protein structure by s ...... magnetic relaxation filtering.
@ast
Probing protein structure by s ...... magnetic relaxation filtering.
@en
type
label
Probing protein structure by s ...... magnetic relaxation filtering.
@ast
Probing protein structure by s ...... magnetic relaxation filtering.
@en
prefLabel
Probing protein structure by s ...... magnetic relaxation filtering.
@ast
Probing protein structure by s ...... magnetic relaxation filtering.
@en
P1433
P1476
P2093
P304
P31
P356
P407
P433
P478
P50
P577
P698
P356
P1433
P1476
Probing protein structure by s ...... magnetic relaxation filtering.
@en
P2093
P304
P31
P356
10.1016/0022-2836(92)90551-T
P407
P433
P478
P50
P577
P698