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Evolution of the folding ability of proteins through functional selection

Authors
  • Seiji Saito
  • Masaki Sasai
  • Tetsuya Yomo
Publisher
The National Academy of Sciences of the USA
Publication Date
Oct 14, 1997
Source
PMC
Keywords
Disciplines
  • Biology
License
Unknown

Abstract

An evolutionary process is simulated with a simple spin-glass-like model of proteins to examine the origin of folding ability. At each generation, sequences are randomly mutated and subjected to a simulation of the folding process based on the model. According to the frequency of local configurations at the active sites, sequences are selected and passed to the next generation. After a few hundred generations, a sequence capable of folding globally into a native conformation emerges. Moreover, the selected sequence has a distinct energy minimum and an anisotropic funnel on the energy surface, which are the imperative features for fast folding of proteins. The proposed model reveals that the functional selection on the local configurations leads a sequence to fold globally into a conformation at a faster rate.

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