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Design of a Monomeric 23-Residue Polypeptide with Defined Tertiary Structure

Struthers, Mary D. and Cheng, Richard P. and Imperiali, Barbara (1996) Design of a Monomeric 23-Residue Polypeptide with Defined Tertiary Structure. Science, 271 (5247). pp. 342-345. ISSN 0036-8075. doi:10.1126/science.271.5247.342.

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Small proteins or protein domains generally require disulfide bridges or metal sites for their stabilization. Here it is shown that the ββα architecture of zinc fingers can be reproduced in a 23-residue polypeptide in the absence of metal ions. The sequence was obtained through an iterative design process. A key feature of the final design is the incorporation of a type II' β turn to aid in β-hairpin formation. Nuclear magnetic resonance analysis reveals that the α helix and β hairpin are held together by a defined hydrophobic core. The availability of this structural template has implications for the development of functional polypeptides.

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Additional Information:© 1996 American Association for the Advancement of Science. Received 17 August 1995; accepted 13 November 1995. This work was supported by NSF grant CHE-910445, a Parsons Foundation predoctoral fellowship (M.D.S.), an NIH traineeship (R.P.C.), and a Camille and Henry Dreyfus Teacher Scholar Award( B.I.). We gratefully acknowledge the Dorothy Chandler, Camilla Chandler Frost Laboratory in Biology at the California Institute of Technology for use of the Varian Unity Plus 600 NMR Spectrometer.
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Parsons FoundationUNSPECIFIED
Camille and Henry Dreyfus FoundationUNSPECIFIED
Issue or Number:5247
Record Number:CaltechAUTHORS:20141215-144428439
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Official Citation:Design of a Monomeric 23-Residue Polypeptide with Defined Tertiary Structure Mary D. Struthers, Richard P. Cheng, and Barbara Imperiali Science 19 January 1996: 271 (5247), 342-345. [DOI:10.1126/science.271.5247.342]
Usage Policy:No commercial reproduction, distribution, display or performance rights in this work are provided.
ID Code:52826
Deposited By: Tony Diaz
Deposited On:15 Dec 2014 23:14
Last Modified:10 Nov 2021 19:44

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