Sponsored by the Rutgers University Department of Mathematics and the
Center for Discrete Mathematics and Theoretical Computer Science (DIMACS)

Andrew Baxter, Rutgers University, baxter{at} math [dot] rutgers [dot] edu
Doron Zeilberger, Rutgers University, zeilberg {at} math [dot] rutgers [dot] edu

Title: Relationship between Amino Acids Sequences and Protein Structures: Folding Patterns and Sequence Patterns

Speaker: Alexander Kister, Rutgers University

Date: Thursday, October 29, 2009 5:00pm

Location: Hill Center, Room 705, Rutgers University, Busch Campus, Piscataway, NJ


A fundamental principle that governs sequence-structure relationship of proteins states that the native structure of a protein is determined by its amino acid sequence. This principle implies that similar sequences encode similar structures. Observations showed that proteins tend to share similar three-dimensional structures when their sequence identity exceeds 30%. This is an important observation because, first, it provides the threshold for structure prediction from amino acid sequences and, secondly, it suggests that a relatively small number of residues in a sequence are critical to structure formation, while others play a relatively minor structural role. Thus, even though each residue makes some contribution to 3D structure formation, the relative weights of the contributions vary greatly. The goal of this research is to develop the method for identification of residues, which play an essential role for structure formation.