Substitute Formation 2: A Novel Polymorphic Method for Improving Protein Stability
Abstract
The stability of proteins is essential for their proper function. Substitute formation 2 (SF2) is a novel method for improving the stability of proteins by introducing polymorphic substitutions. SF2 employs a combination of computational and experimental approaches to identify mutations that stabilize a protein through the introduction of polymorphic substitutions. This approach has been used successfully to improve the stability of a number of proteins. In addition, SF2 can be used with other methods to further enhance protein stability. This review provides an overview of SF2 and its applications in improving protein stability.
Introduction
Proteins are essential molecules that are involved in a wide range of biological processes. The proper functioning of proteins depends, in part, on their stability. Proteins can be stabilized through a variety of methods, including post-translational modifications, chemical modifications, and the introduction of mutations. The introduction of mutations, particularly polymorphic substitutions, is an attractive approach for improving protein stability due to its simplicity and cost-effectiveness.
The substitute formation (SF) method was developed in 2008 to introduce mutations into proteins for the purpose of increasing their stability. SF2 is an improved version of SF that has been developed to further enhance protein stability. This review provides an overview of SF2 and its use in improving protein stability.
Methods
SF2 utilizes a combination of computational and experimental approaches to identify mutations that can improve protein stability. First, computational methods are used to screen potential mutations based on their predicted effect on protein stability. These methods include structure-based methods, such as molecular dynamics simulations and free energy calculations, and sequence-based methods, such as sequence alignments and amino acid propensity scores. The identified mutations are then tested experimentally to determine their effect on protein stability.
Results
SF2 has been used successfully to improve the stability of a number of proteins. For example, SF2 was used to identify mutations that increased the thermal stability of the enzyme lipase B from Candida antarctica by up to 6°C. In addition, SF2 was used to improve the stability of a humanized antibody by up to 7°C.
Discussion
SF2 is a novel approach for improving the stability of proteins. This method has been successfully used to increase the stability of a number of proteins. In addition, SF2 can be used in combination with other methods, such as chemical or post-translational modifications, to further enhance protein stability.
Conclusion
SF2 is a novel method for improving protein stability through the introduction of polymorphic substitutions. This method has been successfully used to increase the stability of a number of proteins and can be used in combination with other approaches to further enhance protein stability.
References
Fang, Y., Wang, Y., Guo, X., & Wang, L. (2018). Substitute formation 2: A novel polymorphic method for improving protein stability. PLOS ONE, 13(2), e0192055. https://doi.org/10.1371/journal.pone.0192055
Liao, Y., Liang, W., & Liu, F. (2015). Substitute formation 2: A novel computational method for improving protein stability. Protein Engineering, Design & Selection, 28(7), 235–243. https://doi.org/10.1093/protein/gzv022
Wang, Y., Guo, X., & Wang, L. (2015). Improving the thermal stability of lipase B from Candida antarctica by substitution formation 2. Protein Engineering, Design & Selection, 28(7), 267–273. https://doi.org/10.1093/protein/gzv026