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Posttranslational mutagenesis: A chemical strategy for exploring protein side-chain diversity

Abstract:

Post-translational modification of proteins expands their structural and functional capabilities beyond those directly specified by the genetic code. However, the vast diversity of chemically-plausible (including unnatural but functionally relevant) side-chains is not readily accessible. We describe C(sp3)–C(sp3) bond-forming reactions on proteins under biocompatible conditions, which exploit unusual carbon free radical chemistry, and use them to form C–C bonds with altered side chains. We ...

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Publication status:
Published
Peer review status:
Peer reviewed

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Publisher copy:
10.1126/science.aag1465

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Institution:
University of Oxford
Division:
MPLS
Department:
Chemistry
Sub department:
Organic Chemistry
Role:
Author
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Institution:
University of Oxford
Division:
MPLS
Department:
Chemistry
Sub department:
Organic Chemistry
Role:
Author
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Funding agency for:
Wright, T
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Funding agency for:
Raj, R
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Funding agency for:
Bower, B
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Funding agency for:
Faulkner, S
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Publisher:
American Association for the Advancement of Science Publisher's website
Journal:
Science Journal website
Publication date:
2016-09-01
Acceptance date:
2016-09-12
DOI:
EISSN:
1095-9203
ISSN:
1095-9203 and 0036-8075
Pmid:
27708059
Source identifiers:
703130
Keywords:
Pubs id:
pubs:703130
UUID:
uuid:9179e0bf-4fb4-4c67-bb52-742087c4be4d
Local pid:
pubs:703130
Deposit date:
2017-07-08

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