| Title | Are natural proteins special? Can we do that? |
| Publication Type | Journal Article |
| Year of Publication | 2018 |
| Authors | Hecht, MH, Zarzhitsky, S, Karas, C, Chari, S |
| Journal | Curr Opin Struct Biol |
| Volume | 48 |
| Pagination | 124-132 |
| Date Published | 2018 Feb |
| ISSN | 1879-033X |
| Keywords | Amino Acid Sequence, Escherichia coli, Escherichia coli Proteins, Gene Deletion, Gene Library, Genetic Complementation Test, Models, Molecular, Protein Binding, Protein Conformation, Protein Conformation, alpha-Helical, Protein Conformation, beta-Strand, Protein Engineering, Protein Folding |
| Abstract | <p>Natural proteins represent a minuscule fraction of possible sequence space. These very rare sequences display remarkable properties: They fold into many different stable structures, and perform a wide range of complex biological functions. These two considerations-rarity and functionality-may suggest that natural proteins are somehow special. Is this true? We address this question by exploring attempts to recapitulate the special structures and functions of natural proteins into sequences designed de novo.</p> |
| DOI | 10.1016/j.sbi.2017.11.009 |
| Alternate Journal | Curr Opin Struct Biol |
| PubMed ID | 29306103 |
