Structure / Function Relationship in Proteins
Understanding the relationship between protein structure and function remains a primary focus in structural biology with important consequences in such diverse fields as molecular biology, genetics, biochemistry, protein engineering and bioinformatics. One approach to this problem is to study how nature has reengineered proteins for new functions through evolutionary processes. This strategy has the potential to reveal fundamental characteristics of protein structures and the explicit manner in which they deliver their associated functions. Between these evolutionary processes, our laboratory has studied the capability to carry out structural transitions disorder-to-order, order-to-disorder of specific protein segments lately recognized as important in the understanding of protein function.
In an attempt to define the possibility that key folding features in proteins could provide us with the manner in which to explain basic issues such as receptor recognition, enzyme activation, lipid transfer activity, and self-exchangeability carried out by several lipid transfer proteins including a series of apolipoproteins, our group has attempted to address these phenomena by directly measuring molecular conformational changes of these molecules in solution modulated by lipids, as well as employing air/water and lipid/water interfaces.