Multiple-site labeling of proteins with unnatural amino acids

Karin V. Loscha; Anthony J. Herlt; Ruhu Qi; Thomas Huber; Kiyoshi Ozawa; Gottfried Otting

doi:10.1002/anie.201108275

Multiple-site labeling of proteins with unnatural amino acids

Karin V. Loscha
, Anthony J. Herlt
, Ruhu Qi
, Thomas Huber
, Kiyoshi Ozawa
, Gottfried Otting^*

^*Corresponding author for this work

Research output: Contribution to journal › Article › peer-review

99 Citations (Scopus)

Abstract

A cell-free protein synthesis system from which the release factor RF1 has been selectively removed enables the facile incorporation of unnatural amino acids into proteins at difficult and multiple sites by optimized use of orthogonal tRNA/aminoacyl-tRNA synthetase systems. ¹⁹F-NMR spectroscopy of a protein labeled combinatorially with trifluoromethyl phenylalanine (red in picture) at multiple sites establishes resonance assignments with a minimal number of samples.

Original language	English
Pages (from-to)	2243-2246
Number of pages	4
Journal	Angewandte Chemie - International Edition
Volume	51
Issue number	9
DOIs	https://doi.org/10.1002/anie.201108275
Publication status	Published - 27 Feb 2012

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title = "Multiple-site labeling of proteins with unnatural amino acids",

abstract = "A cell-free protein synthesis system from which the release factor RF1 has been selectively removed enables the facile incorporation of unnatural amino acids into proteins at difficult and multiple sites by optimized use of orthogonal tRNA/aminoacyl-tRNA synthetase systems. 19F-NMR spectroscopy of a protein labeled combinatorially with trifluoromethyl phenylalanine (red in picture) at multiple sites establishes resonance assignments with a minimal number of samples.",

keywords = "NMR spectroscopy, cell-free protein synthesis, protein modifications, termination factor RF1, unnatural amino acids",

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AU - Loscha, Karin V.

AU - Herlt, Anthony J.

AU - Qi, Ruhu

AU - Huber, Thomas

AU - Ozawa, Kiyoshi

AU - Otting, Gottfried

PY - 2012/2/27

Y1 - 2012/2/27

N2 - A cell-free protein synthesis system from which the release factor RF1 has been selectively removed enables the facile incorporation of unnatural amino acids into proteins at difficult and multiple sites by optimized use of orthogonal tRNA/aminoacyl-tRNA synthetase systems. 19F-NMR spectroscopy of a protein labeled combinatorially with trifluoromethyl phenylalanine (red in picture) at multiple sites establishes resonance assignments with a minimal number of samples.

AB - A cell-free protein synthesis system from which the release factor RF1 has been selectively removed enables the facile incorporation of unnatural amino acids into proteins at difficult and multiple sites by optimized use of orthogonal tRNA/aminoacyl-tRNA synthetase systems. 19F-NMR spectroscopy of a protein labeled combinatorially with trifluoromethyl phenylalanine (red in picture) at multiple sites establishes resonance assignments with a minimal number of samples.

KW - NMR spectroscopy

KW - cell-free protein synthesis

KW - protein modifications

KW - termination factor RF1

KW - unnatural amino acids

UR - https://www.scopus.com/pages/publications/84857508460

U2 - 10.1002/anie.201108275

DO - 10.1002/anie.201108275

M3 - Article

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JO - Angewandte Chemie - International Edition

JF - Angewandte Chemie - International Edition

IS - 9

ER -

Multiple-site labeling of proteins with unnatural amino acids

Abstract

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