Welcome to the Fürtig lab, a young investigator lab at the Institute of Organic Chemistry and Chemical Biology of Goethe University in Frankfurt.
The central themes of our research are the structural dynamics of biopolymers, in particular RNA and protein folding in all its flavors - folding into three-dimensional structures, refolding between multi-stable conformations and unfolding of structures during metabolic processes.
To describe folding reactions of RNAs and proteins either in isolation as well as in their functional macromolecular complexes in terms of kinetic, thermodynamics and structure at atomic resolution, we use NMR spectroscopy as the major experimental tool.
NMR structure of the Vibrio vulnificus ribosomal protein S1 domains D3 and D4 provides insights into molecular recognition of single-stranded RNAs
The ribosomal S1 protein is indispensable for translation initiation in Gram-negative bacteria. rS1 is a multidomain protein that acts as an RNA chaperone and ensures that mRNAs can bind the ribosome in a single-stranded conformation, which could be related to fast recognition. In this paper, we present the NMR solution structure of the minimal mRNA-binding fragment of Vibrio Vulnificus rS1 containing the domains D3 and D4.