Influenza A Matrix Protein1 C Domain Structure and Developments in Nuclear Overhauser Effect Spectroscopy

Nuclear Magnetic Resonance (NMR) spectroscopy provides a platform to study both structure and dynamics of macromolecules, making it an indispensable technique in structural biology. The work described here separately yet collectively complement the importance as well as the ability of solution NMR in structural studies. The first part describes the use of solution state NMR and other biophysical methods in characterizing the structure of micelle bound Influenza A Matrix Protein1 C domain. We have characterized the oligomeric count, affinity and secondary structural changes of the protein upon binding to different lipid environments as micelles and bicelles and its effect with respect to pH and charge. According to our studies at the moment, the Matrix protein1 C domain changes the conformation into a three helical bundle in the presence of membrane. I further discuss the structure statistics in comparison to the experimental data. The second part describes significance of super resolution NOESY, a method developed to improve the quality of NOESY spectroscopy for larger systems, using Influenza hemagglutinin fusion peptide (HAfp) in bicelles system. This is focused to get better resolution while retaining the information, especially distance restraints. I discuss the theory, enhancement according to the experimental data, as well as experimental parameter optimization to reap maximum benefit from the technique.