Bulletin of the American Physical Society
APS March Meeting 2011
Volume 56, Number 1
Monday–Friday, March 21–25, 2011; Dallas, Texas
Abstract: S1.00142 : The Evolutionary Design of Proteins
Author:
Proteins fold spontaneously into precise, well-packed 3D
structures, and execute complex functions such as specificity in
molecular recognition, and efficient catalysis. Despite this,
many studies show that proteins are robust to random mutagenesis.
Additionally, proteins are evolvable. What principles underlying
the design of natural proteins explain these properties? Recent
work examining correlated evolution of amino acid positions shows
that many positions in proteins are nearly statistically
independent while 10-20\% are organized into groups of co-evolving
positions \ \textendash \ termed ``protein sectors'' \textendash
\ that
underlie conserved,
independently varying biological activities. These findings
suggest that the basic design of natural proteins is
fundamentally tied to the nature of fluctuations in the selection
pressures during evolution. We propose to test this hypothesis
using a system for high-speed laboratory evolution and determine
how variation in selection pressures influences the architecture
of amino acid interactions within a protein.
To cite this abstract, use the following reference: http://meetings.aps.org/link/BAPS.2011.MAR.S1.142
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