Designability of α-helical proteins

Eldon G. Emberly, Ned S. Wingreen, Chao Tang

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29 Scopus citations


A typical protein structure is a compact packing of connected α-helices and/or β-strands. We have developed a method for generating the ensemble of compact structures a given set of helices and strands can form. The method is tested on structures composed of four α-helices connected by short turns. All such natural four-helix bundles that are connected by short turns seen in nature are reproduced to closer than 3.6 Å per residue within the ensemble. Because structures with no natural counterpart may be targets for ab initio structure design, the designability of each structure in the ensemble-defined as the number of sequences with that structure as their lowest-energy state-is evaluated using a hydrophobic energy. For the case of four α-helices, a small set of highly designable structures emerges, most of which have an analog among the known four-helix fold families; however, several packings and topologies with no analogs in protein database are identified.

Original languageEnglish (US)
Pages (from-to)11163-11168
Number of pages6
JournalProceedings of the National Academy of Sciences of the United States of America
Issue number17
StatePublished - Aug 20 2002

All Science Journal Classification (ASJC) codes

  • General


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