ABSTRACT
The ultimate aim of structural genomics is to contribute to biology and medicine by correlating protein
structures and activity on one side, and protein misfolding and some diseases on another side. Such an
ambitious goal requires an accurate and detailed knowledge of (1) the 3D architecture of proteins, (2)
conformational changes experienced by proteins in solution around their stable equilibrium structure,
and (3) which of these conformational changes are related to protein functions. Thanks to advances in
x-ray and nuclear magnetic resonance (NMR) technologies, databases devoted to crystal structure of
proteins have dramatically increased in size during the last two decades. Moreover, these studies have
shown that proteins belonging to the same family generally share the same global 3D architecture.
Progress in protein structure modeling is expected to reduce the need for experimental determination of
proteins, focusing only to those that are suspected to have sufficiently novel structures. The current role,
limitations, challenges, and prospects for protein structure modeling (using information about genes
and genomes) have been recently discussed [1].
