Mutation-induced Structural Changes of a Bacterial Protein Detected by MMS

Abstract

The binding affinity of proteins is directly related to their higher order structure (HOS) since the three-dimensional arrangement of the sequence gives rise to binding pockets and protein-protein/nucleic acid interaction scaffolds. The protein studied in this work is involved in bacterial adhesion and is known to change its binding affinity upon mutation in certain domains. Here, we demonstrate that these mutations are associated with structural changes in the protein which can be successfully identified and characterized using Microfluidic Modulation Spectroscopy (MMS).