Site-specific dynamics of amyloid formation and fibrillar configuration of Aβ1–23 using an unnatural amino acid

2015 ◽  
Vol 51 (32) ◽  
pp. 7000-7003 ◽  
Author(s):  
Haiyang Liu ◽  
Richard Lantz ◽  
Patrick Cosme ◽  
Nelson Rivera ◽  
Carlos Andino ◽  
...  
Keyword(s):  
Amino Acid ◽  
Unnatural Amino Acid ◽  
Amyloid Formation ◽  
Site Specific ◽  
Local Dynamics ◽  
Spectroscopic Probe

Distinct local dynamics of Aβ1–23 amyloid formation are characterized using an unnatural amino acid p-cyanophenylalanine as a spectroscopic probe.

scholarly journals Site-Specific Dynamics of Aβ1-23 Amyloid Formation and Fibrillar Configuration using an Unnatural Amino Acid

2015 ◽  
Vol 108 (2) ◽  
pp. 64a ◽  
Author(s):  
Deguo Du ◽  
Haiyang Liu ◽  
Richard Lantz ◽  
Patrick Cosme ◽  
Andrew C. Terentis ◽  
...  
Keyword(s):  
Amino Acid ◽  
Unnatural Amino Acid ◽  
Amyloid Formation ◽  
Site Specific

scholarly journals Generating Permissive Site‐specific Unnatural Amino Acid Synthetases

2010 ◽  
Vol 24 (S1) ◽  
Author(s):  
Ryan A Mehl ◽  
Shigeki J Miyake‐Stoner ◽  
Christian A. Refakis
Keyword(s):  
Amino Acid ◽  
Unnatural Amino Acid ◽  
Site Specific

scholarly journals High-Yield, Zero-Leakage Expression System with a Translational Switch Using Site-Specific Unnatural Amino Acid Incorporation

2013 ◽  
Vol 80 (5) ◽  
pp. 1718-1725 ◽  
Author(s):  
Masaomi Minaba ◽  
Yusuke Kato
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Unnatural Amino Acids ◽  
Mammalian Cells ◽  
Expression System ◽  
Trna Synthetase ◽  
Unnatural Amino Acid ◽  
Translational Efficiency ◽  
Site Specific ◽  
Content Type

ABSTRACTSynthetic biologists construct complex biological circuits by combinations of various genetic parts. Many genetic parts that are orthogonal to one another and are independent of existing cellular processes would be ideal for use in synthetic biology. However, our toolbox is still limited with respect to the bacteriumEscherichia coli, which is important for both research and industrial use. The site-specific incorporation of unnatural amino acids is a technique that incorporates unnatural amino acids into proteins using a modified exogenous aminoacyl-tRNA synthetase/tRNA pair that is orthogonal to any native pairs in a host and is independent from other cellular functions. Focusing on the orthogonality and independency that are suitable for the genetic parts, we designed novel AND gate and translational switches using the unnatural amino acid 3-iodo-l-tyrosine incorporation system inE. coli. A translational switch was turned on after addition of 3-iodo-l-tyrosine in the culture medium within minutes and allowed tuning of switchability and translational efficiency. As an application, we also constructed a gene expression system that produced large amounts of proteins under induction conditions and exhibited zero-leakage expression under repression conditions. Similar translational switches are expected to be applicable also for eukaryotes such as yeasts, nematodes, insects, mammalian cells, and plants.

Site-Specific Analysis of Protein Hydration Based on Unnatural Amino Acid Fluorescence

2015 ◽  
Vol 137 (15) ◽  
pp. 4988-4992 ◽  
Author(s):  
Mariana Amaro ◽  
Jan Brezovský ◽  
Silvia Kováčová ◽  
Jan Sýkora ◽  
David Bednář ◽  
...  
Keyword(s):  
Amino Acid ◽  
Unnatural Amino Acid ◽  
Protein Hydration ◽  
Site Specific ◽  
Specific Analysis

scholarly journals Tetrahydrofuranyl and tetrahydropyranyl protection of amino acid side-chains enables synthesis of a hydroxamate-containing aminoacylated tRNA

2015 ◽  
Vol 13 (8) ◽  
pp. 2341-2349
Author(s):  
Lester J. Lambert ◽  
Marvin J. Miller ◽  
Paul W. Huber
Keyword(s):  
Transcription Factor ◽  
Amino Acid ◽  
Unnatural Amino Acid ◽  
Side Chains ◽  
Site Specific ◽  
Suppressor Trna ◽  
Amino Acid Side Chains

O-protection using tetrahydrofuranyl or tetrahydropyranyl enabled addition of a hydroxamate-containing unnatural amino acid to a suppressor tRNA, allowing subsequent site-specific incorporation of the amino acid into the transcription factor, TFIIIA.

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