Five Heirarchical Levels of Sequence-Structure Correlations in Proteins
Department of Biology
November 8, 2005
Sage 3510 - 4:00 p.m. to 5:00 p.m.
Refreshments at 3:30 p.m.
Expert classification of protein structures hints at the underlying
physical process of protein folding and serves as a guide for a
computational model for folding. Proteins are made up of conserved
short sequence-structure motifs, which are patterns of amino acids that
correlate with structure. These motifs are arranged in such a way along
the chain that suggests a grammatical model, and are arranged in space
in ways that suggest higher-order motifs.
In this talk, I will review about eight years of work on statistical
modeling of sequence-structure correlations in proteins, leading towards
a set of five heirarchical models paralleling the physical process of folding.
The output of each model is the input of the next. Using the analogy of
language models -- the first model condenses characters into words; the
second, words into phrases; the third, phrases into associated pairs of
phrases; the fourth, pairs of phrases into packed assemblies; and the fifth,
packed assemblies into proteins. Molecular simulations based on statistical
models will also be discussed.
Hosted by: Jeff Trinkle (x8291)
Last updated: October 18, 2005