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原文連結
論文資訊
- 類型：已發表論文
- 日期：2014-12-04
摘要
The correspondence between 蛋白質 sequences and structures, or sequence-structure map, relates to fundamental aspects of structural, 演化ary and synthetic biology. The specifics of the mapping, such as the fraction of accessible sequences and structures, or the sequences' ability to fold fast, are dictated by the type of interactions between the monomers that compose the sequences. The set of possible interactions between monomers is encapsulated by the potential energy function. In this study, I explore the impact of the relative forces of the potential on the architecture of the sequence-structure map. My observations rely on simple exact models of 蛋白質s and random samples of the space of potential energy functions of binary alphabets. I adopt a graph perspective and study the distribution of
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