Optimal design of thermally stable proteins.

Bioinformatics
Ryan M BannenJulie C Mitchell

Abstract

For many biotechnological purposes, it is desirable to redesign proteins to be more structurally and functionally stable at higher temperatures. For example, chemical reactions are intrinsically faster at higher temperatures, so using enzymes that are stable at higher temperatures would lead to more efficient industrial processes. We describe an innovative and computationally efficient method called Improved Configurational Entropy (ICE), which can be used to redesign a protein to be more thermally stable (i.e. stable at high temperatures). This can be accomplished by systematically modifying the amino acid sequence via local structural entropy (LSE) minimization. The minimization problem is modeled as a shortest path problem in an acyclic graph with nonnegative weights and is solved efficiently using Dijkstra's method.

References

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Datasets Mentioned

BETA
GM074901-01
GM064598

Methods Mentioned

BETA
ICE

Software Mentioned

Sun Fire X4100 Linux
ICE
MERLTG

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