VB: Ph.D. position NMR Sweden Biophysical Chemistry/Biochemistry

PhD-position in Chemistry with focus on Biophysical


Umeå University, Faculty of Science and Technology www.umu.se

Contact: Gerhard Gröbner, Dept of Chemistry, Umeå University,Gerhard.grobner@chem.umu.se

Link to ad http://umu.mynetworkglobal.com/what:job/jobID:121609/

This PhD position is part of a project where we apply biophysical and biochemical methods to understand how nature removes dysfunctional, infected and superfluous cells through a strictly controlled process known as programmed cell death (apoptosis). The main research task is the use of a variety of NMR methods to provide a structural understanding of the molecular mechanism by which opposite acting proteins from the apoptosis regulating Bcl-2 family interact with biological membranes.

Application deadline is 2016-12-19.


This PhD position is part of a research project where we will explore how the regulation of programmed cell death occurs with focus on the structure of the proteins and biological membranes involved in this vital process. The main control system of the mitochondrial (intrinsic) pathway of cell death are membrane-active proteins of the Bcl-2 family. Members of this family, who have opposing functions, meet at the mitochondrial outer membrane, where they will determine whether a cell should live or die.

The main goal of this project is to understand the function - and the underlying structural characteristics - of these proteins and their interactions with the mitochondrial membrane environment. For this purpose we will use a range of biophysical / biochemical methods with focus on solid-state NMR spectroscopy of lipid/protein complexes. By applying advanced solid-state NMR methods we will be able to provide a structural insight into the molecular mechanism by which the pro-survival Bcl-2 membrane protein and its opponent, the cell killing Bax protein, interact at the mitochondrial membrane and thereby determine the fate of a cell.

Applicants should first study the function and structure of the membrane-bound Bcl-2 protein and its structural changes upon its inhibition by the Bax protein; a task that will also include functional studies, including the influence of membrane lipids on the structure of the Bcl-2 protein. The labb provides access to an excellent research infrastructure within the KBC environment (www.kbc.umu.se) with access to solid-state/