The research field of the Iwahara lab is biophysical chemistry of protein-DNA interactions. The current main projects in the lab are as follows:
Mechanisms of DNA scanning by proteins
When transcription factors and DNA repair/modifying enzymes perform their function, these molecules must first locate their specific target sites in the vast presence of nonspecific but structurally similar sites on DNA. How do proteins scan DNA? Using NMR spectroscopy, stopped flow fluorescence spectroscopy, and other biophysical / biochemical methods along with mutagenesis, the Iwahara lab is investigating how proteins scan DNA and locate their target sites.
Ion-pair dynamics and their role in protein-DNA association
Ion-pair formation is one of the most fundamental chemical interactions for life. Despite their potential importance in molecular recognition and enzymatic catalysis, the dynamics of ion pairs of biological macromolecules are not well understood. Recently the Iwahara group has developed unique NMR methods for investigating dynamics of ion pairs involving protein side chains. Using these methods, the lab is elucidating the role of ion-pair dynamics in protein-DNA interactions.
Nuclear Magnetic Resonance (NMR) spectroscopy is an important tool for our reserach. The Iwahara group is a major user of UTMB's NMR facility, where three Bruker Avance-III NMR spectrometers operated at the 1H frequencies of 600, 750, and 800 MHz are available. The 800- and 750-MHz spectrometers are equipped with TCI (1H/2H/13C/15N) cryoprobes, and the 600-MHz spectrometer is equipped with a QCI (1H/2H/13C/15N/31P) cryoprobe. In addition to standard heteronuclear multi-dimensional NMR pulse sequences, the group uses its own pulse sequences developed for its research.