The roles of unfolded states of proteins in normal folding and in diseases involving
aggregation, as well as the prevalence and regulatory functions of intrinsically disordered …

NMR spectroscopy is a key method for studying the structure and dynamics of (large)
multidomain proteins and complexes in solution. It plays a unique role in integrated …

Macromolecular structures calculated from nuclear magnetic resonance data are not fully
determined by experimental data but depend on subjective choices in data treatment and …

Structural biology is rapidly accumulating a wealth of detailed information about protein
function, binding sites, RNA, large assemblies and molecular motions. These data are …

Abstract Src‐homology 3 (SH3) domains recognize PXXP core motif preceded or followed
by positively charged residue (s). Whether SH3 domains recognize motifs other than proline …

Enteropathogenic Escherichia coli (EPEC) induce gross cytoskeletal rearrangement within
epithelial cells, immediately beneath the attached bacterium. The C-terminal 280 amino acid …

The N-terminal SH3 domain of drk (drkN SH3) is unstable, existing in equilibrium between a
folded state (Fexch) and an unfolded state (Uexch) under non-denaturing buffer conditions …

Various strategies are described and compared for measurement of one-bond JNH and
JNC′ splittings in larger proteins. In order to evaluate the inherent resolution obtainable in …

1. Introduction.................................................................. 172 1.1. Advantages of isotope
labelling................................................ 172 1.2. Labelling requirements for solid-state …

Battling metastasis through inhibition of cell motility is considered a promising approach to
support cancer therapies. In this context, Ena/VASP-depending signaling pathways, in …