Didem VARDAR ULU

As a biophysical chemist, I like to understand why things are the way they are, and how they do what they do at a molecular level. In particular, I am intrigued by the rules that govern macromolecular structure, dynamics, and folding, especially of proteins, as they pertain to function and regulation. In my laboratory, we combine a variety of biophysical and biochemical methods to study molecular structure, conformational change, protein stability, and intermolecular interactions, such as ligand binding. Since most of the proteins involved in important biological pathways are large multi-domain proteins, making it challenging to study them at a molecular level, we heavily rely on protein dissection methodology, where a multi-domain protein is studied as an assembly of structurally independent, small functional units that can be characterized in isolation. The molecular level information about these isolated domains can then be transferred or applied to other proteins with similar domains.

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The overall goal for the projects in my laboratory is to fill the existing gaps in our understanding of the sequence-structure-function relationship for small proteins or protein domains within their relevant specific biological background and also provide new insights into our global understanding of protein folding and stability. Our current focus is on two protein domains from the Negative Regulatory Region of the multi-domain developmental protein, Notch Receptor: Lin12/Notch Repeats (LNRs) and the Heterodimerizatin Domain (HD)