19-23 November, 2018
Rosario, Argentina
“Proteins sample a wide variety of environments in vivo. Depending on its sub-cellular localization they are exposed to different degrees of macromolecular crowding, varied pH values and/or experience transient interactions with other cellular components such as metabolites, lipidic membranes, nucleic acids and proteins. In addition they can be post-translationally modified in response to precise cellular stimuli and in a time dependent manner. These diverse conditions and environments modulate dramatically protein structure and function. Accordingly, proteins can be understood only under conditions similar to those for which they were selected, the so-called physiological state. However, most protein structural studies are typically performed on isolated samples, under conditions that differ substantially from in vivo environments of live cells. The question arises whether protein features observed in vitro correlate with their in vivo behaviors?
In this course we will introduce to you state of the art In-cell NMR techniques to characterize proteins in their native environments. We will present applications to study the structure, folding and dynamics of proteins inside live cells as well as cellular biology process of biological relevance. The theoretical modules include the basic principles of NMR spectroscopy, sample preparation for In-cell studies and In-cell NMR data acquisition and analysis. There will be two practical modules including the recording of in-cell NMR spectra and monitoring of biologically relevant protein-post translational modifications.”
