about
A natural and readily available crowding agent: NMR studies of proteins in hen egg whiteIn-cell NMR: an emerging approach for monitoring metal-related events in living cells.Perspectives on NMR in drug discovery: a technique comes of agePeeking into living eukaryotic cells with high-resolution NMR.Specific ion effects on macromolecular interactions in Escherichia coli extracts.Protein folding and unfolding studied at atomic resolution by fast two-dimensional NMR spectroscopyNMR in pharmacokinetic and pharmacodynamic profiling.Recent progress in NMR spectroscopy: toward the study of intrinsically disordered proteins of increasing size and complexity.In-cell NMR and EPR spectroscopy of biomacromolecules.Solution NMR Spectroscopy in Target-Based Drug Discovery.Functional binding surface of a β-hairpin VEGF receptor targeting peptide determined by NMR spectroscopy in living cells.Effects of recombinant protein expression on green fluorescent protein diffusion in Escherichia coli.In NMR tube transcription for rapid screening of RNA conformation.Detecting intracellular cysteine redox states by in-cell NMR spectroscopy.NMR spectroscopic studies of intrinsically disordered proteins at near-physiological conditions.Mapping functional interaction sites of human prune C-terminal domain by NMR spectroscopy in human cell lysates.In-cell NMR: from metabolites to macromolecules.
P2860
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P2860
description
im August 2005 veröffentlichter wissenschaftlicher Artikel
@de
wetenschappelijk artikel
@nl
наукова стаття, опублікована в серпні 2005
@uk
name
In-Cell NMR Spectroscopy
@en
In-Cell NMR Spectroscopy
@nl
type
label
In-Cell NMR Spectroscopy
@en
In-Cell NMR Spectroscopy
@nl
prefLabel
In-Cell NMR Spectroscopy
@en
In-Cell NMR Spectroscopy
@nl
P2860
P356
P1433
P1476
In-Cell NMR Spectroscopy
@en
P2093
Frank Löhr
Sina Reckel
P2860
P304
P356
10.1002/CBIC.200500076
P577
2005-08-03T00:00:00Z