Incorporation of Non-Canonical Amino Acids

Lilia Leisle; Francis Valiyaveetil; Ryan A. Mehl; Christopher A. Ahern

doi:10.1007/978-1-4939-2845-3_7

Incorporation of Non-Canonical Amino Acids

Lilia Leisle, Francis Valiyaveetil, Ryan A. Mehl, Christopher A. Ahern

Physiology & Pharmacology

Research output: Contribution to journal › Review article › peer-review

15 Scopus citations

Abstract

In this chapter we discuss the strengths, caveats and technical considerations of three approaches for reprogramming the chemical composition of selected amino acids within a membrane protein. In vivo nonsense suppression in the Xenopus laevis oocyte, evolved orthogonal tRNA and aminoacyl-tRNA synthetase pairs and protein ligation for biochemical production of semisynthetic proteins have been used successfully for ion channel and receptor studies. The level of difficulty for the application of each approach ranges from trivial to technically demanding, yet all have untapped potential in their application to membrane proteins.

Original language	English (US)
Pages (from-to)	119-151
Number of pages	33
Journal	Advances in experimental medicine and biology
Volume	869
DOIs	https://doi.org/10.1007/978-1-4939-2845-3_7
State	Published - 2015

Keywords

Evolved tRNA synthetase pairs
Intein ligation
Nonsense suppression
Protein semi-synthesis

ASJC Scopus subject areas

Biochemistry, Genetics and Molecular Biology(all)

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10.1007/978-1-4939-2845-3_7

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abstract = "In this chapter we discuss the strengths, caveats and technical considerations of three approaches for reprogramming the chemical composition of selected amino acids within a membrane protein. In vivo nonsense suppression in the Xenopus laevis oocyte, evolved orthogonal tRNA and aminoacyl-tRNA synthetase pairs and protein ligation for biochemical production of semisynthetic proteins have been used successfully for ion channel and receptor studies. The level of difficulty for the application of each approach ranges from trivial to technically demanding, yet all have untapped potential in their application to membrane proteins. ",

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author = "Lilia Leisle and Francis Valiyaveetil and Mehl, {Ryan A.} and Ahern, {Christopher A.}",

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T1 - Incorporation of Non-Canonical Amino Acids

AU - Leisle, Lilia

AU - Valiyaveetil, Francis

AU - Mehl, Ryan A.

AU - Ahern, Christopher A.

PY - 2015

Y1 - 2015

N2 - In this chapter we discuss the strengths, caveats and technical considerations of three approaches for reprogramming the chemical composition of selected amino acids within a membrane protein. In vivo nonsense suppression in the Xenopus laevis oocyte, evolved orthogonal tRNA and aminoacyl-tRNA synthetase pairs and protein ligation for biochemical production of semisynthetic proteins have been used successfully for ion channel and receptor studies. The level of difficulty for the application of each approach ranges from trivial to technically demanding, yet all have untapped potential in their application to membrane proteins.

AB - In this chapter we discuss the strengths, caveats and technical considerations of three approaches for reprogramming the chemical composition of selected amino acids within a membrane protein. In vivo nonsense suppression in the Xenopus laevis oocyte, evolved orthogonal tRNA and aminoacyl-tRNA synthetase pairs and protein ligation for biochemical production of semisynthetic proteins have been used successfully for ion channel and receptor studies. The level of difficulty for the application of each approach ranges from trivial to technically demanding, yet all have untapped potential in their application to membrane proteins.

KW - Evolved tRNA synthetase pairs

KW - Intein ligation

KW - Nonsense suppression

KW - Protein semi-synthesis

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DO - 10.1007/978-1-4939-2845-3_7

M3 - Review article

C2 - 26381943

AN - SCOPUS:84955151935

VL - 869

SP - 119

EP - 151

JO - Advances in Experimental Medicine and Biology

JF - Advances in Experimental Medicine and Biology

SN - 0065-2598

ER -

Incorporation of Non-Canonical Amino Acids

Abstract

Keywords

ASJC Scopus subject areas

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