NMR spectroscopy is a powerful tool for biologists interested in the structure, dynamics, and
interactions of biological macromolecules. This review aims at presenting in an accessible …

The past decades of advancements in NMR have made it a very powerful tool for metabolic
research. Despite its limitations in sensitivity relative to mass spectrometric techniques, NMR …

A method for elucidating the relative configuration of acyclic organic compounds was
developed on the basis of carbon− proton spin-coupling constants (2, 3 JC, H) and …

Aminoglycoside antibiotics that bind to 30 S ribosomal A-site RNA cause misreading of the
genetic code and inhibit translocation. The aminoglycoside antibiotic paromomycin binds …

A common RXL motif waa found in proiine-rich iigands that were selected from a blased
combinatorial peptide library on the basis of their ability to bind specifically to the SH3 …

The introduction of nuclear magnetic resonance (NMR) spectroscopy as a second method
for protein structure determination at atomic resolution, in addition to x-ray diffraction in …

The nuclear factor CREB activates transcription of target genes in part through direct
interactions with the KIX domain of the coactivator CBP in a phosphorylation-dependent …

Protein–ligand interactions are of fundamental importance in almost all processes in living
organisms. The ligands comprise small molecules, drugs or biological macromolecules and …

The 3D solution structure of the GCC‐box binding domain of a protein from Arabidopsis
thaliana in complex with its target DNA fragment has been determined by heteronuclear …

NMR is very well suited to the study of especially weak protein− protein interactions, as no
crystallization is required. The available NMR methods to this end are reviewed and …