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Engineered protein function by selective amino acid diversification
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DOI：10.1016/j.ymeth.2003.10.004.png)
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Abstract
En 中文
Almost all protein engineering methods rely upon making changes to naturally occurring proteins that already possess some of the desired properties. This will probably remain the case as long as we lack a complete understanding of the way that an amino acid sequence gives rise to a protein with a precisely defined biological function. Common to all methods for altering an existing protein is the selection of a subset of amino acids in the protein for variation and a choice of which substitutions to make at each position. Variants are then tested empirically and further variants are created based upon their performance. Differences between protein engineering methods arc the ways in which amino acids are chosen for variation, the protocols followed for creating the variants, and how information regarding variant properties is used in creating subsequent variants. In this article, we describe these differences and provide examples of how the experimental parameters of specific projects determine which method is most suitable. (C) 2003 Elsevier Inc. All rights reserved.
Keywords:
IN-VITRO RECOMBINATION
DNA SHUFFLING METHOD
SIGNAL-TRANSDUCTION
DIRECTED EVOLUTION
RANDOM CHIMERAGENESIS
GUANYLYL CYCLASE
GENETIC SCREENS
MUTATIONS
KINASE
IDENTIFICATION