Protein design by binary patterning of polar and nonpolar amino acids

Satwik Kamtekar, Jarad M. Schiffer, Huayu Xiong, Jennifer M. Babik, Michael H. Hecht

Research output: Contribution to journalArticlepeer-review

678 Scopus citations


A general strategy is described for the de novo design of proteins. In this strategy the sequence locations of hydrophobic and hydrophilic residues were specified explicitly, but the precise identities of the side chains were not constrained and varied extensively. This strategy was tested by constructing a large collection of synthetic genes whose protein products were designed to fold into four-helix bundle proteins. Each gene encoded a different amino acid sequence, but all sequences shared the same pattern of polar and nonpolar residues. Characterization of the expressed proteins indicated that most of the designed sequences folded into compact α-helical structures. Thus, a simple binary code of polar and nonpolar residues arranged in the appropriate order can drive polypeptide chains to collapse into globular α-helical folds.

Original languageEnglish (US)
Pages (from-to)1680-1685
Number of pages6
Issue number5140
StatePublished - 1993
Externally publishedYes

All Science Journal Classification (ASJC) codes

  • General


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