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Rational Protein Engineering Guided by Deep Mutational Scanning

Department of Biological Sciences and KI for the BioCentury, Korea Advanced Institute of Science and Technology (KAIST), Daejeon 305-701, Korea
Author to whom correspondence should be addressed.
Academic Editor: Qiang “Shawn” Chen
Int. J. Mol. Sci. 2015, 16(9), 23094-23110;
Received: 14 August 2015 / Revised: 4 September 2015 / Accepted: 13 September 2015 / Published: 23 September 2015
(This article belongs to the Special Issue Protein Engineering)
Sequence–function relationship in a protein is commonly determined by the three-dimensional protein structure followed by various biochemical experiments. However, with the explosive increase in the number of genome sequences, facilitated by recent advances in sequencing technology, the gap between protein sequences available and three-dimensional structures is rapidly widening. A recently developed method termed deep mutational scanning explores the functional phenotype of thousands of mutants via massive sequencing. Coupled with a highly efficient screening system, this approach assesses the phenotypic changes made by the substitution of each amino acid sequence that constitutes a protein. Such an informational resource provides the functional role of each amino acid sequence, thereby providing sufficient rationale for selecting target residues for protein engineering. Here, we discuss the current applications of deep mutational scanning and consider experimental design. View Full-Text
Keywords: deep mutational scanning; next generation sequencing; high-throughput screening; protein engineering deep mutational scanning; next generation sequencing; high-throughput screening; protein engineering
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Shin, H.; Cho, B.-K. Rational Protein Engineering Guided by Deep Mutational Scanning. Int. J. Mol. Sci. 2015, 16, 23094-23110.

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