热稳定性
蛋白质工程
突变
计算生物学
定向进化
蛋白质设计
蛋白质稳定性
序列(生物学)
定向分子进化
计算机科学
化学
生物
突变
蛋白质结构
酶
生物化学
基因
突变体
作者
Hein J. Wijma,R.J. Floor,Dick B. Janssen
标识
DOI:10.1016/j.sbi.2013.04.008
摘要
Protein engineering strategies for increasing stability can be improved by replacing random mutagenesis and high-throughput screening by approaches that include bioinformatics and computational design. Mutations can be focused on regions in the structure that are most flexible and involved in the early steps of thermal unfolding. Sequence analysis can often predict the position and nature of stabilizing mutations, and may allow the reconstruction of thermostable ancestral sequences. Various computational tools make it possible to design stabilizing features, such as hydrophobic clusters and surface charges. Different methods for designing chimeric enzymes can also support the engineering of more stable proteins without the need of high-throughput screening.
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