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Science. 1988 Aug 19;241(4868):976-8.

Characterization of a helical protein designed from first principles.

Author information

1
E. I. du Pont de Nemours & Company, Central Research & Development Department, Wilmington, DE 19898.

Abstract

The question of how the primary amino acid sequence of a protein determines its three-dimensional structure is still unanswered. One approach to this problem involves the de novo design of model peptides and proteins that should adopt desired three-dimensional structures. A systematic approach was aimed at the design of a four-helix bundle protein. The gene encoding the designed protein was synthesized and the protein was expressed in Escherichia coli and purified to homogeneity. The protein was shown to be monomeric, highly helical, and very stable to denaturation by guanidine hydrochloride (GuHCl). Thus a globular protein has been designed that is capable of adopting a stable, folded structure in aqueous solution.

PMID:
3043666
[Indexed for MEDLINE]

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