Susanne Ressl

Susanne Ressl

Assistant Scientist, Molecular and Cellular Biochemistry

  • suressl@indiana.edu
  • 812/856-5801
  • Simon Hall 200C
  • Office Hours
    M-F
    By Appointment Only

Education

  • Otto-Hahn Fellowship, Max-Planck Society Germany, 2012-2014
  • EMBO Longterm Fellowship, -, 2010-2011
  • Postdoctoral Fellow, Structural Neuroscience , Stanford University, 2010-2014
  • Ph.D., Biochemistry, Biophysics, Max-Planck Institute of Biophysics, University of Frankfurt, Germany, 2009
  • M.S., Biophysics, Immunology, Zoology , University of Mainz, Germany, Honors Thesis at the Max-Planck Institute of Biophysics, 2006
  • B.S., University of Mainz (Germany)-Biology , 2003

About

Structure Biology allows us to look and analyze a protein’s three-dimensional structure and defer functional information from it. Biochemistry allows us to analyze a protein’s chemical properties and its physiological relevance on a chemical level. The powerful combination of both advances our understanding of molecular mechanisms of protein machineries on an atomic level. Solving the structure - function relationship of a protein enables the discovery of unexpected relationships between different protein families and can aid in the design of therapeutic strategies.

The Ressl lab focuses on solving protein structures, in particular membrane proteins. Membrane proteins are a fascinating class of proteins. Embedded in the cell’s membrane, they are the vital link between outside and inside world and facilitate various crucial physiological functions. Functions such as: 1) transporters, transporting molecules or ions across the membrane, 2) anchors, anchoring proteins and providing cell stability and interacting with cell matrix proteins, 3) receptors and enzyme that provide major signalling functions in the cell, such as G-protein coupled receptors that are involved in the majority of physiological functions.

Membrane proteins are involved in all aspects of physiological processes, therefore it is not surprising that about 40% of our genome encodes for membrane proteins. However, compared to the number of crystal structures of soluble proteins (~72000), membrane protein structures (~310) are underrepresented in the structure database.

The Ressl lab seeks to solve crystal structures of membrane protein targets that will increase our understanding of mechanisms of: a) ion and small molecule transport, b) cell adhesion and signaling and c) regulation of membrane lipid compositions in bacterial and mammalian systems. We also work on method development in membrane protein X-ray crystallography.