Seminar

Analysis and Prediction of Protein Structure Based on Delaunay Tessellation

Dr. Alex Tropsha
School of Pharmacy
University of North Carolina
Chapel Hill, NC

Monday, October 13, 1997
3:00 pm
3269 Beckman Institute

Delaunay tessellation of a protein (using united C-alpha atom representation of individual residues) generates an aggregate of space-filling, irregular tetrahedra (Delaunay simplices). Statistical analysis of quadruplet residue compositions of all Delaunay simplices in a representative dataset of protein structures leads to a novel four-body nearest neighbor residue potential derived from individual scores for all quadruplets of natural amino acids. Delaunay tessellation provides new measures of sequence-structure compatibility. For instance, 3D-1D Delaunay tessellation profiles can distinguish between correct and (even slightly) erroneous folds (e.g., structure refinement, homology modeling). Delaunay tessellation also provides a new graphical tool for protein structure analysis which allows one to locate and visualize structural cores of folded proteins.

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