Evolutionary Information Hidden in a Single Protein Structure
| Autor: | Chang, Chih-Min, 張智閔 |
|---|---|
| Rok vydání: | 2012 |
| Druh dokumentu: | 學位論文 ; thesis |
| Popis: | 100 Protein residues that are critical for structure and function that are expect-ing to be conserved throughout evolution. Finding the conserved residues might be helpful in understanding the mechanism of chemical reaction or information of protein folding. Generating the conservation profile of a sequence requires aligning families of homologous sequences and having knowledge of their evo-lutionary relationships. Here, we report that the conservation profile at the resi-due level can be quantitatively derived from a single protein structure with only backbone information. We found that the reciprocal packing density profiles of protein structures closely resemble their sequence conservation profiles. For a set of 554 non-homologous enzymes, 74% (408/554) of the proteins have a cor-relation coefficient > 0.5 between these two profiles. Our main result is the es-tablishment of a close correlation between a protein’s conservation profile and its packing density profile on the level of individual proteins. Later, We found that the elucidation of the evolutionary coupling among subunits based on the comparison of two profiles. Finally, we made a discussion on why evolutionary information could be derived from only a single protein structure. |
| Databáze: | Networked Digital Library of Theses & Dissertations |
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