Arne Elofsson, Department of Biochemistry, University of Stockholm
One of the fundamental question that remain to solve in todays molecular bilogy is "How does protein fold ?". This can be divided into two parts, (1) We do not fully understand the physics about protein folding and would like to understand that better. (2) We want to put all crystallographer out of work and be able to predict the structure of a protein by hand (or with the help of a computer). The last question become increasingly more important as the gap between the number of known protein sequences and protein structures increases through the progress of all genome projects.
The best (only ?) method to predict the structure of a protein from its sequence is by finding a protein with a structure is already known that has a similar structure to the protein of interest. If there is such a protein with a high sequence similarity the problem is solved and one can move onto the problem of homology modelling.
Many proteins with apparently unrelated sequences have been found to have very similar 3-dimensional structures. This has lead to the development of methods to detect the fold of a sequence from a library of known folds. Some of these methods are based solely on sequence information , others on multiple aligned sequences , others on structural information and still others on predicted properties of protein structures.
In this lecture I will outline the yesterday, today and future of protein fold recognition.
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