1521-3773/asset/cover.gif?v=1&s=412bc65bdcb3f0e34a94f27c1c13e908726694d4 "Angewandte Chemie International Edition")
J.C. and A.S. are supported by the Wellcome Trust (Grant number GR064417MA). J.C. is a Wellcome Trust Senior Research Fellow. A.B. is supported by a fellowship from Istituto Pasteur—Fondazione Cenci Bolognetti (Rome). We thank Dr. Robert Best for helpful comments on our design.
1521-3773/asset/2002_left.gif?v=1&s=ac6b0d94a94d7ce7a210002b8096b42feffc0bcf)
1521-3773/asset/2002_right.gif?v=1&s=451042aa3415ae3ad0729984d26dee1866aca82e)
Communication
You have full text access to this OnlineOpen article
An Effective Strategy for the Design of Proteins with Enhanced Mechanical Stability†
Article first published online: 29 JUL 2008
DOI: 10.1002/anie.200801761
Copyright © 2008 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim
Additional Information
How to Cite
Borgia, A., Steward, A. and Clarke, J. (2008), An Effective Strategy for the Design of Proteins with Enhanced Mechanical Stability. Angew. Chem. Int. Ed., 47: 6900–6903. doi: 10.1002/anie.200801761
- †
Publication History
- Issue published online: 20 AUG 2008
- Article first published online: 29 JUL 2008
- Manuscript Received: 15 APR 2008
Funded by
- Wellcome Trust. Grant Number: GR064417MA
- Istituto Pasteur—Fondazione Cenci Bolognetti
Keywords:
- Force microscopy;
- mechanical properties;
- protein engineering;
- titin
Titinic strength: The mechanical resistance of titin domain I27 (see picture, left) was increased by substituting residues from a stronger homologue in regions of the protein important for mechanical strength (red). The unfolding profile of I27st (see picture, right) shows that the mechanical strength is significantly increased compared to wild-type I27 (black arrow).