NMR spectroscopy is arguably the most powerful tool for the study of molecular structures
and interactions, and is increasingly being applied to environmental research, such as the …

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

MARS a program for robust automatic backbone assignment of 13 C/15 N labeled proteins
is presented. MARS does not require tight thresholds for establishing sequential connectivity …

Transient macromolecular complexes are often formed by protein–protein interaction
domains (eg PDZ, SH2, SH3, WW) which recognize linear sequence motifs with in vitro …

Toxin–antitoxin systems are highly abundant in plasmids and bacterial chromosomes. They
ensure plasmid maintenance by killing bacteria that have lost the plasmid. Their expression …

In this chapter, we summarize the isotopic labeling strategies used to obtain high-quality
solution and solid-state NMR spectra of biological samples, with emphasis on integral …

Contents 1. Introduction............................................................................. 33 1.1. Automated
structure determination methods in the postgenomics area.............................. 34 2. Automated …

Intrinsically disordered proteins (IDPs) are characterized by highly flexible solvent exposed
backbones and can sample many different conformations. These properties confer them …

A crucial step in determining solution structures of proteins using nuclear magnetic
resonance (NMR) spectroscopy is the process of sequential assignment, which correlates …

Although there is great interest in three-dimensional structures of glycoproteins and complex
oligosaccharides, their structural determination have been hampered by inhomogeneous …