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In vitro evolution of thermodynamically stable turns

Nature Structural Biology volume 3, pages 446–451 (1996)Cite this article

Abstract

To determine the role of primary structure in specifying turns, random sequences (guests) were substituted for the native turn sequences in a series of proteins (hosts) of differing thermo-dynamic stabilities.The fraction of inserts that result in active proteins is measured as a function of the stability of the host and temperature. With a highly stable host more than half of the inserts give functional proteins. However, a smaller fraction of sequences supports folding as the stability of the host decreases, and the temperature increases. The sequences of many of the selected inserts resemble the wild-type turn, and those that diverge match other established turn preferences. Thermodynamic measurements show that turn sequences selected under stringent conditions result in the most stable proteins. Thus, β-turns appear to be under evolutionary pressure favouring thermodynamically stable structures.

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Author notes

  1. William F. DeGrado

    Present address: Department of Biochemistry & Biophysics, University of Pennsylvania School of Medicine, Philadelphia, Pennsylvania, 19104-6059, USA

Authors and Affiliations

  1. DuPont Merck Pharmaceutical Company, The Experimental Station, P.O. Box 80336, Wilmington, Delaware, 19880-0336, USA

    Hongxing X. Zhou, Ronald H. Hoess & William F. DeGrado

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  1. Hongxing X. Zhou
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  2. Ronald H. Hoess
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  3. William F. DeGrado
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Zhou, H., Hoess, R. & DeGrado, W. In vitro evolution of thermodynamically stable turns. Nat Struct Mol Biol 3, 446–451 (1996). https://doi.org/10.1038/nsb0596-446

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