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proteins (8) 8
index medicus (5) 5
nuclear magnetic resonance spectroscopy (5) 5
spectroscopy (5) 5
polarization (4) 4
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hyperpolarization (3) 3
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Journal Article
Angewandte Chemie International Edition, ISSN 1433-7851, 08/2016, Volume 55, Issue 36, pp. 10526 - 10526
Directing hyperpolarization to a target protein makes it possible to selectively filter out signals of specific proteins from a large background. In their... 
cell lysates | structural biology | structure elucidation | NMR spectroscopy | proteins | Proteins | Signal to noise ratio | Polarization | Lysates | Nuclear magnetic resonance--NMR | Hyperpolarization
Journal Article
Biophysical Journal, ISSN 0006-3495, 04/2018, Volume 114, Issue 7, p. 1614
Intrinsically disordered proteins dynamically sample a wide conformational space and therefore do not adopt a stable and defined three-dimensional... 
Proteins | Medical research | Molecular dynamics | Physiological aspects | Medicine, Experimental | Nuclear magnetic resonance spectroscopy | Protein binding
Journal Article
Frontiers in molecular biosciences, ISSN 2296-889X, 2019, Volume 6, pp. 13 - 13
Barttin is an accessory subunit of ClC-K chloride channels expressed in the kidney and the inner ear. Main functions of ClC-K/barttin channels are the... 
lipid bilayer nanodisc | ion channel | detergent micelle | barttin | nuclear magnetic resonance
Journal Article
Biophysical Journal, ISSN 0006-3495, 04/2018, Volume 114, Issue 7, pp. 1614 - 1623
Intrinsically disordered proteins dynamically sample a wide conformational space and therefore do not adopt a stable and defined three-dimensional... 
UNSTRUCTURED PROTEINS | INTRINSICALLY DISORDERED PROTEINS | MOLECULAR-DYNAMICS | STRUCTURAL ENSEMBLES | DYNAMIC NUCLEAR-POLARIZATION | BIOPHYSICS | PHOSPHOLIPID-BILAYER | RANDOM COIL | FORCE-FIELD | UNFOLDED PROTEINS | MEMBRANE-PROTEIN | Index Medicus | Proteins
Journal Article
Journal Article
Angewandte Chemie, ISSN 0044-8249, 08/2016, Volume 128, Issue 36, pp. 10904 - 10908
Nuclear magnetic resonance (NMR) spectroscopy has the intrinsic capabilities to investigate proteins in native environments. In general, however, NMR relies on... 
Strukturaufklärung | Proteine | Strukturbiologie | Zelllysate | NMR-Spektroskopie | Proteins | Nuclear magnetic resonance spectroscopy | Spectroscopy | Polarization | Biotechnology | Dynamics | Ligands | Nuclear magnetic resonance | Radicals
Journal Article
Angewandte Chemie, ISSN 0044-8249, 08/2016, Volume 128, Issue 36, p. 10904
  Nuclear magnetic resonance (NMR) spectroscopy has the intrinsic capabilities to investigate proteins in native environments. In general, however, NMR relies... 
Proteins | Nuclear magnetic resonance--NMR | Signal to noise ratio | Enrichment | Cell culture | Polarization | Spectroscopy | Purity | Selectivity | Radicals | Lysates | Protein folding | Resonance | Protein interaction | Hyperpolarization
Journal Article
Angewandte Chemie, ISSN 0044-8249, 08/2016, Volume 128, Issue 36, pp. 10682 - 10682
Mit Hyperpolarisation, die zu einem Zielprotein gelenkt wird, ist es möglich, die Signale bestimmter Proteine von Hintergrundsignalen zu trennen. In der... 
Strukturaufklärung | Proteine | Strukturbiologie | Zelllysate | NMR-Spektroskopie
Journal Article
Communications biology, ISSN 2399-3642, 2018, Volume 1, Issue 1, pp. 44 - 44
The protein α-Synuclein (αS) is linked to Parkinson's disease through its abnormal aggregation, which is thought to involve cytosolic and membrane-bound forms... 
Journal Article
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