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Rational Design to Improve Protein Thermostability: Recent Advances and Prospects
Author(s) -
Yang Haiquan,
Liu Long,
Li Jianghua,
Chen Jian,
Du Guocheng
Publication year - 2015
Publication title -
chembioeng reviews
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.089
H-Index - 22
ISSN - 2196-9744
DOI - 10.1002/cben.201400032
Subject(s) - thermostability , protein stability , protein engineering , rational design , thermal stability , biochemical engineering , protein design , disulfide bond , materials science , chemistry , nanotechnology , computer science , protein structure , engineering , biochemistry , enzyme , organic chemistry
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.