Phyloseminar: David Liberles speaks March 28th on “Protein Structural, Biophysical, and Genomic Underpinnings of Protein Sequence Evolution”

"Protein Structural, Biophysical, and Genomic Underpinnings of Protein
Sequence Evolution"
David Liberles (U Wyoming)

Common models for amino acid substitution assume that each site
evolves independently according to average properties in the absence
of a genomic, protein structural or functional context. Two
characterizations of amino acid substitution will be presented. One
approach extends a population genetic model to inter-specific genomic
data and a second approach evaluates the effects of selection for
protein folding and protein-protein interaction on sequence evolution.
Several take home lessons include the importance of considering
linkage independent of protein structure, the importance of negative
pleiotropy (or not statements in folding and binding), and the nature
of the co-evolution of sites and how it links standard substitution
models with covarion models when binding function is conserved and
when it changes.

West Coast USA: 13:00 (01:00 PM) on Wednesday, March 28
East Coast USA: 16:00 (04:00 PM) on Wednesday, March 28
England: 21:00 (09:00 PM) on Wednesday, March 28
France: 22:00 (10:00 PM) on Wednesday, March 28
Japan: 05:00 (05:00 AM) on Thursday, March 29
New Zealand: 09:00 (09:00 AM) on Thursday, March 29

http://phyloseminar.org/

Author: Jonathan Eisen

I am an evolutionary biologist and a Professor at U. C. Davis. (see my lab site here). My research focuses on the origin of novelty (how new processes and functions originate). To study this I focus on sequencing and analyzing genomes of organisms, especially microbes and using phylogenomic analysis

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