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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
Version:
Accepted manuscript

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Publisher copy:
10.1126/science.aag1465

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Department:
Oxford, MPLS, Chemistry, Organic Chemistry
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Author
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Department:
Oxford, MPLS, Chemistry, Organic Chemistry
Role:
Author
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Funding agency for:
Wright, TH
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Funding agency for:
Bower, BJ
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Funding agency for:
Raj, R
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Funding agency for:
Faulkner, SC
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Publisher:
American Association for the Advancement of Science Publisher's website
Journal:
Science Journal website
Publication date:
2016-09-05
Acceptance date:
2016-09-12
DOI:
EISSN:
1095-9203
ISSN:
0036-8075 and 1095-9203
Pubs id:
pubs:703130
URN:
uri:9179e0bf-4fb4-4c67-bb52-742087c4be4d
UUID:
uuid:9179e0bf-4fb4-4c67-bb52-742087c4be4d
Local pid:
pubs:703130
Keywords:

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