The structure of the compounds was assigned by IR and NMR spectroscopy.

We have determined the structure of the free PBX homeodomain using NMR spectroscopy.

Here we report the three-dimensional structure of human CXCR1 determined by NMR spectroscopy.

We describe structural studies of the C-peptide using 2D NMR spectroscopy.

Using NMR spectroscopy, we identified the biosynthetic product as MEL-A with altered sugar conformation.

Here we present a three-dimensional structure of this protein as determined by NMR spectroscopy.

NMR spectroscopy confirmed the cross-linker synthesis and the preservation of the active maleimide function.

The compounds were characterised by NMR spectroscopy and X-ray crystallography.

The induced asymmetry is consistent with the complex's solution properties as determined using NMR spectroscopy.

Their structures were determined by MS and NMR spectroscopies.

The structures of synthesized compounds were fully characterized by multinuclear NMR spectroscopy and X-ray crystallography.

For some toxins, the three-dimensional structure has been solved by X-ray diffraction and NMR spectroscopy.

Structural compositions of the conjugates were verified by 1H NMR spectroscopy and CHN elemental analyses.

The structures of the esters were elucidated by means of spectral data, including 2D NMR spectroscopy.

NMR spectroscopy provides evidence of intramolecular hydrogen bonding under physiological conditions in two of the inhibitors.

Our NMR spectroscopy data indicated that the presence of D137L introduced long range rearrangements in TM structure.