Mapping structural interactions using in-cell NMR spectroscopy (STINT-NMR)

Mapping protein-protein interactions in solution by NMR spectroscopy.

NMR is very well suited to the study of especially weak protein-protein interactions, as no crystallization is required. The available NMR methods to this end are reviewed and illustrated with applications from the recent biochemical literature: intermolecular NOEs, cross-saturation, chemical shift perturbation, dynamics and exchange perturbation, paramagnetic methods, and dipolar orientation. ...

In-cell NMR spectroscopy.

In-Cell Biochemistry Using NMR Spectroscopy

Biochemistry and structural biology are undergoing a dramatic revolution. Until now, mostly in vitro techniques have been used to study subtle and complex biological processes under conditions usually remote from those existing in the cell. We developed a novel in-cell methodology to post-translationally modify interactor proteins and identify the amino acids that comprise the interaction surfa...

The structural analysis of protein-protein interactions by NMR spectroscopy.

A comprehensive understanding of protein-protein interactions is an important next step in our quest to understand how the information contained in a genome is put into action. Although a number of experimental techniques can report on the existence of a protein- protein interaction, very few can provide detailed structural information. NMR spectroscopy is one of these, and in recent years seve...

The Keratan Sulphates: Structural Investigations Using Nmr Spectroscopy