Posttranslational mutagenesis: A chemical strategy for exploring protein side-chain diversity-Reference-Cited by-同舟云学术

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

Published:2016-11-04 Issue:6312 Volume:354 Page:
ISSN:0036-8075
Container-title:Science
language:en
Short-container-title:Science

Author:

Wright Tom H.¹,Bower Ben J.¹,Chalker Justin M.¹,Bernardes Gonçalo J. L.¹,Wiewiora Rafal¹,Ng Wai-Lung¹,Raj Ritu¹,Faulkner Sarah¹,Vallée M. Robert J.¹,Phanumartwiwath Anuchit¹,Coleman Oliver D.¹,Thézénas Marie-Laëtitia²,Khan Maola¹,Galan Sébastien R. G.¹,Lercher Lukas¹,Schombs Matthew W.¹,Gerstberger Stefanie¹,Palm-Espling Maria E.¹,Baldwin Andrew J.¹,Kessler Benedikt M.²,Claridge Timothy D. W.¹,Mohammed Shabaz¹,Davis Benjamin G.¹

Affiliation:

1. Department of Chemistry, University of Oxford, Oxford OX1 3TA, UK.

2. Target Discovery Institute, Nuffield Department of Medicine, University of Oxford, Headington, Oxford OX3 7FZ, UK.

Abstract

Radicals push proteins beyond genes Chemically modifying proteins after their translation can expand their structural and functional roles (see the Perspective by Hofmann and Bode). Two related methods describe how to exploit free radical chemistry to form carbon-carbon bonds between amino acid residues and a selected functional group. Wright et al. added a wide range of functional groups to proteins containing dehydroalanine precursors, with borohydride mediating the radical chemistry. Yang et al. employed a similar approach, using zinc in combination with copper ions. Together, these results will be useful for introducing functionalities and labels to a wide range of proteins. Science , this issue pp. 597 and 623 ; see also p. 553

Funder

Felix Foundation

Croucher Foundation

Rutherford Foundation

Cancer Research UK

BBSRC

AstraZeneca

UCB

EPSRC

Royal Society Wolfson Research Merit Award

Publisher

American Association for the Advancement of Science (AAAS)