| 摘要 |
A general method is described for the design and production of a multiplicity of novel proteins. The method entails constructing a degenerate family of synthetic genes wherein each codon is chosen to specify either a polar or a non-polar amino acid, but the exact identity of the amino acid at each particular position is not specified explicitly. Thus a huge collection of different proteins can be encoded using a simple binary code of polar versus non-polar amino acids. The periodicity of the polar and non-polar amino acids in the sequence is constrained to match the natural repeat of 3.6 residues/turn in (alpha)-helices. Thus all the novel proteins are explicitly designed to have only hydrophobic amino acids in their interiors, and only hydrophilic amino acids on their surfaces. The synthetic genes encoding these novel proteins are cloned and expressed in vivo, thus giving rise to a library of novel proteins, each of which is easily purified in large quantities. |
