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To characterize the determinants and implications of protein dynamics, there exists no more suited biophysical technique than nuclear magnetic resonance (NMR) spectroscopy.
A partially disordered protein with two Zn finger domains, the work presented here describes the isolation of a GTSF1 protein construct amendable to study by NMR spectroscopy.
The types of analyses conducted on a fee-for-service basis include acquisition and analysis of the required spectra for the elucidation of small molecule structures (includes synthetic molecules, natural products, cofactors, lipids, and short peptides (30 amino acids or less)).
The types of projects conducted collaboratively include the determination of three-dimensional structures of biological macromolecules, including proteins and nucleic acids, both alone and as complexes with various ligands.
This has produced a gap in this area which these webpages aim to bridge by describing the concepts of assignment in detail with the help of many illustrations.
Much space and discussion is devoted to practical aspects.