Volume 2, Issue 2 pp. 87-94
Review

Rational Design to Improve Protein Thermostability: Recent Advances and Prospects

Haiquan Yang

Haiquan Yang

Key Laboratory of Carbohydrate Chemistry and Biotechnology, Ministry of Education, Jiangnan University, 1800 Lihu Road, Wuxi 214122, China.

Key Laboratory of Industrial Biotechnology, Ministry of Education, Jiangnan University, 1800 Lihu Road, Wuxi 214122, China.

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Long Liu

Long Liu

Key Laboratory of Carbohydrate Chemistry and Biotechnology, Ministry of Education, Jiangnan University, 1800 Lihu Road, Wuxi 214122, China.

Key Laboratory of Industrial Biotechnology, Ministry of Education, Jiangnan University, 1800 Lihu Road, Wuxi 214122, China.

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Jianghua Li

Jianghua Li

Key Laboratory of Carbohydrate Chemistry and Biotechnology, Ministry of Education, Jiangnan University, 1800 Lihu Road, Wuxi 214122, China.

Key Laboratory of Industrial Biotechnology, Ministry of Education, Jiangnan University, 1800 Lihu Road, Wuxi 214122, China.

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Jian Chen

Jian Chen

National Engineering of Laboratory for Cereal Fermentation Technology, Jiangnan University, Wuxi 214122, China.

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Guocheng Du

Corresponding Author

Guocheng Du

Key Laboratory of Carbohydrate Chemistry and Biotechnology, Ministry of Education, Jiangnan University, 1800 Lihu Road, Wuxi 214122, China.

Key Laboratory of Industrial Biotechnology, Ministry of Education, Jiangnan University, 1800 Lihu Road, Wuxi 214122, China.

Key Laboratory of Carbohydrate Chemistry and Biotechnology, Ministry of Education, Jiangnan University, 1800 Lihu Road, Wuxi 214122, China.Search for more papers by this author
First published: 11 March 2015
Citations: 69

Abstract

Research on proteins is in rapid development, but the use of wild-type proteins under industrial conditions has limitations, low thermostability in particular. Thermal stability includes three types: thermodynamic, kinetic, and process stability. Several factors (e.g., hydrophobic interactions and hydrogen bonds) affect the thermostability of proteins. The use of rational design to improve protein thermal stability is a hot topic in the field of computational biology and protein engineering. Several methods have been applied successfully to improve the thermal stability of protein, including introducing the number of disulfide bonds, optimizing protein surface charge, homologous comparison, and optimizing the free energy of unfolding. This review summarizes recent advances in our understanding of the factors influencing protein thermostability, highlights its effective improvement strategies, and discusses future prospects in this field.

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