Molecular Modelling Applied to NMR Structure Determination

The Xplor-NIH NMR molecular structure determination package.

We announce the availability of the Xplor-NIH software package for NMR biomolecular structure determination. This package consists of the pre-existing XPLOR program, along with many NMR-specific extensions developed at the NIH. In addition to many features which have been developed over the last 20 years, the Xplor-NIH package contains an interface with a new programmatic framework written in C...

Using Xplor–NIH for NMR molecular structure determination

Introduction to Nmr and Its Application in Metabolite Structure Determination

The broad utility of nuclear magnetic resonance (NMR) was first recognized in 1951 from a series of experiments that observed a relationship between chemical structure and corresponding shifts in the NMR resonances. Since that time, NMR has evolved from continuous wave (CW) spectroscopy to Fourier transform (FT) spectroscopy, from permanent magnets to super conducting magnets and from one dimen...

Automation of NMR structure determination of proteins.

The automation of protein structure determination using NMR is coming of age. The tedious processes of resonance assignment, followed by assignment of NOE (nuclear Overhauser enhancement) interactions (now intertwined with structure calculation), assembly of input files for structure calculation, intermediate analyses of incorrect assignments and bad input data, and finally structure validation...

Protein structure determination from NMR chemical shifts.

NMR spectroscopy plays a major role in the determination of the structures and dynamics of proteins and other biological macromolecules. Chemical shifts are the most readily and accurately measurable NMR parameters, and they reflect with great specificity the conformations of native and nonnative states of proteins. We show, using 11 examples of proteins representative of the major structural c...