We are interested in studying and understanding the basic principles underlying protein packing, folding and stability as well as in applying this knowledge to address biologically relevant problems. We have previously developed methods for the semi-rational design of temperature-sensitive and cold-sensitive mutants of globular proteins and validated these in diverse organisms such as bacteria, yeast and fruit flies. We are currently exploring how combinations of saturation mutagenesis and deep sequencing can be used to rapidly elucidate sequence-structure-function relationships and to guide protein structure prediction. The lab has also developed methodology for specific activation of bacterial toxin-antitoxin systems and is studying their contribution to bacterial persistence. Another major focus of research involves immunogen design to elicit neutralizing antibodies against two important viral pathogens, HIV-1 and influenza.