scholarly journals Diverse Protein Manipulations with Genetically Encoded Glutamic Acid Benzyl Ester

2021 ◽  
Author(s):  
Xiaochen Yang ◽  
Hui Miao ◽  
Ruotong Xiao ◽  
Luyao Wang ◽  
Yan Zhao ◽  
...  

Site-specific modification of proteins has significantly advanced the use of protein in biological research and therapeutics development. Among various strategies aimed at this end, genetic code expansion (GCE) allows structurally...

2016 ◽  
Vol 55 (52) ◽  
pp. 15931-15931
Author(s):  
Ivana Nikić ◽  
Gemma Estrada Girona ◽  
Jun Hee Kang ◽  
Giulia Paci ◽  
Sofya Mikhaleva ◽  
...  

2016 ◽  
Vol 55 (52) ◽  
pp. 16172-16176 ◽  
Author(s):  
Ivana Nikić ◽  
Gemma Estrada Girona ◽  
Jun Hee Kang ◽  
Giulia Paci ◽  
Sofya Mikhaleva ◽  
...  

2014 ◽  
Vol 50 (30) ◽  
pp. 4007-4009 ◽  
Author(s):  
F. C. Wu ◽  
H. Zhang ◽  
Q. Zhou ◽  
M. Wu ◽  
Z. Ballard ◽  
...  

Building biotin-functionalized virus-like particles by combining a genetic code expanding technology and site specific modification of tobacco mosaic virus coat protein.


Biomolecules ◽  
2020 ◽  
Vol 10 (4) ◽  
pp. 578 ◽  
Author(s):  
Jan-Erik Hoffmann

Genetic code expansion is a powerful tool for the study of protein interactions, as it allows for the site-specific incorporation of a photoreactive group via non-canonical amino acids. Recently, several groups have published bifunctional amino acids that carry a handle for click chemistry in addition to the photo-crosslinker. This allows for the specific labeling of crosslinked proteins and therefore the pulldown of peptides for further analysis. This review describes the properties and advantages of different bifunctional amino acids, and gives an overview about current and future applications.


2019 ◽  
Vol 15 (3) ◽  
pp. 276-284 ◽  
Author(s):  
Maximilian Fottner ◽  
Andreas-David Brunner ◽  
Verena Bittl ◽  
Daniel Horn-Ghetko ◽  
Alexander Jussupow ◽  
...  

BIOspektrum ◽  
2021 ◽  
Vol 27 (6) ◽  
pp. 616-619
Author(s):  
Nikolaj Georg Koch ◽  
Nediljko Budisa

AbstractPyrrolysyl-tRNA synthetase (PylRS) is an enzyme of some methanogenic Archaea for the natural incorporation of pyrrolysine into proteins. The discovery of PylRS as a natural tool for genetic code expansion paved the way for site-specific incorporation of non-canonical amino acids (ncAAs) into proteins, with versatile side chains useful in biotechnology. Almost 20 years after the discovery, we describe the journey which led to three distinct classes of PylRSs with unique ncAA recognitions.


2016 ◽  
Vol 27 (10) ◽  
pp. 2460-2468 ◽  
Author(s):  
Yiming Wu ◽  
Hua Zhu ◽  
Bo Zhang ◽  
Fei Liu ◽  
Jingxian Chen ◽  
...  

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