Multidimensional NMR spectroscopy has been established as an indispensible tool for
studying structure, dynamics, and interactions of biopolymers. When used in the frame of a …

Automated methods for protein structure determination by NMR have increasingly gained
acceptance and are now widely used for the automated assignment of distance restraints …

Chemical shift assignment is vital for nuclear magnetic resonance (NMR)–based studies of
protein structures, dynamics, and interactions, providing crucial atomic-level insight …

Conventional protein structure determination from nuclear magnetic resonance data relies
heavily on side-chain proton-to-proton distances. The necessary side-chain resonance …

The new FLYA automated resonance assignment algorithm determines NMR chemical shift
assignments on the basis of peak lists from any combination of multidimensional through …

This work presents the automated projection spectroscopy (APSY) method for the recording
of discrete sets of j projections from N-dimensional (N≥ 3) NMR experiments at operator …

Fully automated structure determination of proteins in solution (FLYA) yields, without human
intervention, three-dimensional protein structures starting from a set of multidimensional …

The recent expansion of structural genomics has increased the demands for quick and
accurate protein structure determination by NMR spectroscopy. The conventional strategy …

In this chapter we describe the core Protein Production Platform of the Northeast Structural
Genomics Consortium (NESG) and outline the strategies used for producing high-quality …

An approach is described for joint interleaved recording, real-time processing, and analysis
of NMR data sets. The method employs multidimensional decomposition to find common …