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Cited by 255

The DOI matches its Crossref record; 40 of the 40 references it cites were found in a registry or an index.

Optimizing non-natural protein function with directed evolution

Open access
Brustad, Eric M, Arnold, Frances H·2011·Current Opinion in Chemical Biology

Abstract

Developing technologies such as unnatural amino acid mutagenesis, non-natural cofactor engineering, and computational design are generating proteins with novel functions; these proteins, however, often do not reach performance targets and would benefit from further optimization. Evolutionary methods can complement these approaches: recent work combining unnatural amino acid mutagenesis and phage selection has created useful proteins of novel composition. And weak initial activity in a computationally designed enzyme has been improved by iterative rounds of mutagenesis and screening. A marriage of ingenuity and evolution will expand the scope of protein function well beyond Mother Nature’s designs.

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Metadata

Authors
Brustad, E. M., & Arnold, F. H.
Venue
Current Opinion in Chemical Biology
Publisher
Elsevier BV
Published
2011-04
Volume
15
Issue
2
Pages
201-210
ISSN
1367-5931 (ISSN-L)
OpenAlex
W2077933693
Cited by
255
References
40
FWCI
1.22
Type
journal article
Language
en
Open access
bronze

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CoChat. (2026). Citation check: Optimizing non-natural protein function with directed evolution. https://app.cochat.ai/papers/10.1016/j.cbpa.2010.11.020
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Brustad, E. M., & Arnold, F. H. (2011). Optimizing non-natural protein function with directed evolution. Current Opinion in Chemical Biology. https://doi.org/10.1016/j.cbpa.2010.11.020

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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).

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