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- W2024485146 abstract "Protein engineering provides a swift and precise means for exploring a protein's structure and activity; however, the effects of these mutations on protein structure and stability cannot be predicted with a comparable precision yet. This chapter discusses on how α-helices pack together to form tertiary structure through redesigning the hydrophobic core of the four-helix-bundle, Rop, and quantifies, the β-sheet forming tendencies of the amino acids using the IgG Fc binding domain of Streptococcal Protein G (β1) as a model system. The chapter discusses that the repacked protein shows significantly increased thermo-stability relative to the wild-type protein. Thus, protein engineering can improve on the natural design, perhaps because the natural protein has evolved to optimize its function rather than its stability. The similarities between the different experimentally measured scales for the β-sheet propensities demonstrate that, there are intrinsic differences in how readily each amino acid can be accommodated in a β-sheet. Future studies will investigate the structural basis of the observed differences in β-sheet propensities, and explore how these differences can be modulated by local environmental effects." @default.
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- W2024485146 date "1995-01-01" @default.
- W2024485146 modified "2023-09-23" @default.
- W2024485146 title "Studying α-helix and β-sheet formation in small proteins" @default.
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- W2024485146 doi "https://doi.org/10.1016/s1080-8914(06)80040-2" @default.
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