In the Spring of 2013, NMR spectroscopists convened at the Weizmann Institute in Israel to
brainstorm on approaches to improve the sensitivity of NMR experiments, particularly when …

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

Recent advances in NMR methodology and techniques allow the structural investigation of
biomolecules of increasing size with atomic resolution. NMR spectroscopy is especially well …

The invention of multidimensional techniques in the 1970s revolutionized NMR, making it
the general tool of structural analysis of molecules and materials. In the most straightforward …

Proteins provide much of the scaffolding for life, as well as undertaking a variety of essential
catalytic reactions. These characteristic functions have led us to presuppose that proteins …

NMR spectroscopy is one of the most powerful and versatile analytic tools available to
chemists. The discrete Fourier transform (DFT) played a seminal role in the development of …

Intrinsically disordered proteins (IDPs) have recently attracted the attention of the scientific
community because of their peculiar features that expand our view of how protein function is …

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) …

Biomolecular force fields optimized for globular proteins fail to properly reproduce properties
of intrinsically disordered proteins. In particular, parameters of the water model need to be …

Two novel 5D NMR experiments (CACONCACO, NCOCANCO) for backbone assignment of
disordered proteins are presented. The pulse sequences exploit relaxation properties of the …