Biomolecular NMR, Drug Design, Membrane Proteins

Ligand binding pocketStructural elucidation of large bio-molecular complexes for rational drug design is the major goal of our research. It is fascinating how tightly dynamically controlled protein-protein interactions affect each and every step of the life cycle. We’d like to develop an understanding of how the information associated with essential biological events is mediated at atomic level and to utilize new paradigms for facilitated design of novel therapeutics.

Solution NMR spectroscopy is an especially powerful technique for examining protein-protein interactions and their dynamic properties at near-physiological conditions. In the post genomic era it is both our privilege and our obligation to make sense of the vast amounts of data generated by sequencing efforts.

Based on the completed genomic analyses of microorganisms, membrane proteins account for about one-third of all the proteins. However, despite recent explosive advances in structural biology the number of membrane protein structures solved each year is limited. Even though complete structure determination of integral membrane proteins by solution NMR remains challenging, it is now feasible to investigate a wide variety of extremely important membrane-associated targets involved in cellular signal transduction.


The aim of this Special Issue is to highlight how recent advances in X-ray crystallography, cryo-EM and nuclear magnetic resonance (NMR) may allow us to shrink this knowledge gap and to provide novel ideas for therapeutics development, particularly keeping in mind that a large portion of drug targets belong to the above class of proteins.

We are pleased to invite you to submit your original research articles as well as comprehensive reviews. Research areas may include (but are not limited to) the following topics related to membrane proteins:

  • Structural studies, correlated with functional states;
  • Investigations of lipid binding/bilayer associations;  
  • Cross-membrane signaling, post-translational modifications; 
  • Characterization of dynamics or order/disorder transitions upon ligand binding or mutations;
  • Introduction of novel membrane mimetics.

We look forward to publishing your outstanding work in this Special Issue.