Protein disulfide engineering.

Alan A Dombkowski, Kazi Zakia Sultana, Douglas B Craig

Journal: FEBS letters 2014;588(2):206-12

PMID: 24291258

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.

Address: Carman and Ann Adams Department of Pediatrics, Wayne State University School of Medicine, Detroit, MI 48201, USA. Electronic address: [email protected].; Department of Computer Science & Engineering, Chittagong University of Engineering & Technology, Chittagong 4349, Bangladesh.; Carman and Ann Adams Department of Pediatrics, Wayne State University School of Medicine, Detroit, MI 48201, USA.

DOI: 10.1016/j.febslet.2013.11.024

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MeSH Terms: Computers, Disulfides, Kinetics, Protein Engineering, Protein Stability, Proteins