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FEBS Lett. 2014 Jan 21;588(2):206-12. doi: 10.1016/j.febslet.2013.11.024. Epub 2013 Nov 26.

Protein disulfide engineering.

Author information

1
Carman and Ann Adams Department of Pediatrics, Wayne State University School of Medicine, Detroit, MI 48201, USA. Electronic address: domski@wayne.edu.
2
Department of Computer Science & Engineering, Chittagong University of Engineering & Technology, Chittagong 4349, Bangladesh.
3
Carman and Ann Adams Department of Pediatrics, Wayne State University School of Medicine, Detroit, MI 48201, USA.

Abstract

Improving the stability of proteins is an important goal in many biomedical and industrial applications. A logical approach is to emulate stabilizing molecular interactions found in nature. Disulfide bonds are covalent interactions that provide substantial stability to many proteins and conform to well-defined geometric conformations, thus making them appealing candidates in protein engineering efforts. Disulfide engineering is the directed design of novel disulfide bonds into target proteins. This important biotechnological tool has achieved considerable success in a wide range of applications, yet the rules that govern the stabilizing effects of disulfide bonds are not fully characterized. Contrary to expectations, many designed disulfide bonds have resulted in decreased stability of the modified protein. We review progress in disulfide engineering, with an emphasis on the issue of stability and computational methods that facilitate engineering efforts.

KEYWORDS:

Disulfide; Engineering; Kinetics; Protein; Stability; Thermodynamics

PMID:
24291258
DOI:
10.1016/j.febslet.2013.11.024
[Indexed for MEDLINE]
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