Interaction proteomics by using 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...

In-cell NMR spectroscopy.

Structural Proteomics by NMR

Nuclear magnetic resonance (NMR) is a powerful spectroscopic technique that permits the detailed study at atomic resolution of the three-dimensional structure and dynamics of macromolecules and their complexes in solution. In this brief chapter, I discuss various aspects of NMR that are pertinent to structural proteomics, that is, the high-throughput study of protein–protein complexes at the at...

Site-Specific Identification of an Aβ Fibril–Heparin Interaction Site by Using Solid-State NMR Spectroscopy**

At the surface of Aβ(1-40) amyloid fibrils that have a threefold molecular symmetry (green in the left picture) a site of interaction of the glycosaminoglycan analogue heparin (blue) was identified. The binding site consists of residues at the N terminus and the turn regions defining the apices of the triangular geometry. Heparin has a lower affinity for Aβ(1-40) fibrils having twofold molecula...

proteomics study of polyethylenimine interaction with cell surface proteins in human colon adenocarcinoma cell line