| Article ID | Journal | Published Year | Pages | File Type |
|---|---|---|---|---|
| 10871309 | FEBS Letters | 2012 | 5 Pages |
Abstract
⺠De novo emergence of proteins is modeled using translated random DNA sequences. ⺠Aggregation, disorder and transmembrane propensities estimated with consensus methods. ⺠GC-content of underlying DNA governs structural preferences of random proteins. ⺠Extant proteins have more transmembrane segments than random ones. ⺠Disorder and aggregation of random proteins is in the range observed for extant ones.
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Authors
Annamária F. Ángyán, András Perczel, Zoltán Gáspári,