Intrinsically disordered proteins (IDPs) are characterized by substantial conformational
plasticity. Given their inherent structural flexibility X-ray crystallography is not applicable to …

Thanks to recent improvements in NMR spectrometer hardware and pulse sequence design,
modern 13C NMR has become a useful tool for biomolecular applications. The complete …

NMR spectroscopy is a versatile tool for studying time-dependent processes: chemical
reactions, phase transitions or macromolecular structure changes. However, time-resolved …

Nuclear magnetic resonance (NMR) spectroscopy is a powerful technique for characterizing
biomolecules such as proteins and nucleic acids at atomic resolution. Increased magnetic …

Thanks to recent improvements in NMR instrumentation, pulse sequence design, and
sample preparation, a panoply of new NMR tools has become available for atomic …

Structural disorder of functional proteins under physiological conditions is widespread within
eukaryotic proteomes. The lack of stable tertiary and secondary structure offers a variety of …

The accurate and precise measurement of one-bond scalar and residual dipolar coupling
(RDC) constants is of prime importance to be able to use RDCs for structure determination. If …

We outline NMR protocols for site-specific mapping and time-resolved monitoring of protein
phosphorylation reactions using purified kinases and mammalian cell extracts. These …

Studies over the past decade have highlighted the functional significance of intrinsically
disordered proteins (IDPs). Due to conformational heterogeneity and inherent dynamics …

The transcription factor ASCIZ (ATMIN, ZNF822) has an unusually high number of
recognition motifs for the product of its main target gene, the hub protein LC8 (DYNLL1) …