Disulfides are generally viewed as structurally stabilizing elements in proteins. However, emerging evidence shows that a subclass of disulfides in proteins may act as redox-controlled switches governing conformational changes in proteins. We are currently characterising these disulfides and their resident proteins using bioinformatic and computational chemistry techniques.Read more
The Gentrepid server uses human genome sequence data and structural bioinformatics tools to predict candidate disease genes for inherited diseases. Input your own disease intervals and Gentrepid will identify candidates or look at the precomputed results for selected diseases.
EGF domains are found singly or in tandem in many mosaic proteins. Two structurally different types of EGF domain exist that are likely to have evolved specific functions. For example, many EGF posttranslational modifications, such as hydroxylation, occur differentially on the two types. Find which type exists in your protein.
How do enzymes evolve? What is the molecular basis of specificity? Can an aminopeptidase become a carboxypeptidase? Is it possible for catalytic residues to change without "killing" the enzyme? We pursue the answers to these questions and more through the technique of ancestral reconstruction and other bioinformatic tools. See group publications
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