NUScon: a community-driven platform for quantitative evaluation of nonuniform sampling in NMR.

Although the concepts of nonuniform sampling (NUS​​​​​​​) and non-Fourier spectral reconstruction in multidimensional NMR began to emerge 4 decades ago , it is only relatively recently that NUS has become more commonplace. Advantages of NUS include the ability to tailor experiments to reduce data collection time and to improve spectral quality, whether through detection of closely spaced peaks (i.e.

Framework for and evaluation of bursts in random sampling of multidimensional NMR experiments.

The grouping of data in bursts, also referred to as clusters, spikes or clumps, is a common phenomenon in stochastic sampling. There have been several reports that suggest that in NMR, the presence of such bursts is beneficial to spectral reconstruction where data are sampled nonuniformly. In this work, we seek to define a mode of sampling that produces bursts of randomly distributed data in a controlled manner.

A non-uniform sampling approach enables studies of dilute and unstable proteins.

NMR spectroscopy is a powerful method in structural and functional analysis of macromolecules and has become particularly prevalent in studies of protein structure, function and dynamics. Unique to NMR spectroscopy is the relatively low constraints on sample preparation and the high level of control of sample conditions. Proteins can be studied in a wide range of buffer conditions, e.

ArachnoServer: a database of protein toxins from spiders.

Background: Venomous animals incapacitate their prey using complex venoms that can contain hundreds of unique protein toxins. The realisation that many of these toxins may have pharmaceutical and insecticidal potential due to their remarkable potency and selectivity against target receptors has led to an explosion in the number of new toxins being discovered and characterised. From an evolutionary perspective, spiders are the most successful venomous animals and they maintain by far the largest pool of toxic peptides.