结构生物学sturcture biology explore-43.pdfVIP

441 Energy estimation in protein design Joaquim Mendes*, Raphael Guerois† and Luis Serrano‡ The progress achieved by several groups in the field of being less sensitive to errors or atom displacement in the computational protein design shows that successful design protein structure. In the case of protein design, however, methods include two major features: efficient algorithms to pairwise statistical potentials for residue–residue inter- deal with the combinatorial exploration of sequence space and actions may not be adequate for the structural stringency optimal energy functions to rank sequences according to their that is required [2,3]. An elegant method has been fitness for the given fold. developed that may overcome this limitation [4]. The four-body statistical potential SNAPP was developed Addresses based on the Delaunay tessellation of protein structure. *European Molecular Biology Laboratory, Meyerhofstrasse 1, The protein structure is divided into tetrahedra whose D-69117 Heidelberg, Germany; e-mail: mendes@embl-heidelberg.de edges represent all nearest neighbors of sidechain centroids. † SBPM-DBCM, CEA Saclay, 91191 Gif sur Yvette Cedex, France; Quite strong correlations were obtained for the prediction e-mail: guerois@cea.fr ‡ European Molecular Biology Laboratory, Meyerhofstrasse 1, of point mutations of hydrophobic residues. Future D-69117 Heidelberg, Germany;