A radical approach to posttranslational mutagenesis
Introducing diverse protein side chains via carbon-carbon bond-forming reactions The structure and function of proteins is extensively modulated and expanded by posttranslational modifications (PTMs) on many of the canonical amino acids. As a means of unraveling the role and interplay of PTMs, metho...
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Published in | Science (American Association for the Advancement of Science) Vol. 354; no. 6312; pp. 553 - 554 |
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Main Authors | , |
Format | Journal Article |
Language | English |
Published |
United States
The American Association for the Advancement of Science
04.11.2016
|
Subjects | |
Online Access | Get full text |
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Summary: | Introducing diverse protein side chains via carbon-carbon bond-forming reactions
The structure and function of proteins is extensively modulated and expanded by posttranslational modifications (PTMs) on many of the canonical amino acids. As a means of unraveling the role and interplay of PTMs, methods to produce proteins with site-specific modifications have attracted considerable attention. In addition to PTMs, incorporation of unnatural side chains is of interest for protein engineering, and systematic studies using analogs of amino acids offer insights into the molecular mechanisms by which proteins and enzymes work. On pages
597
and
623
of this issue, Wright
et al.
(
1
) and Yang
et al.
(
2
) report potentially general strategies to chemically introduce a wide variety of natural, unnatural, posttranslationally modified, and labeled side chains via an unprecedented carbon-carbon bond-forming reaction on intact proteins. This approach will be of particular interest to chemical biologists aiming to introduce authentic protein PTMs, as well as to protein chemists interested in introducing unnatural side chains of their choice. |
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Bibliography: | ObjectType-Article-1 SourceType-Scholarly Journals-1 ObjectType-Feature-2 content type line 23 |
ISSN: | 0036-8075 1095-9203 |
DOI: | 10.1126/science.aai8788 |