ncAA Database
Displaying 1 - 25 of 29 results
ncAA Name | ncAA Structure | ncAA Utility | Moderation State |
---|---|---|---|
p-acetyl-l-phenylalanine | ![]() |
Site-directed spin labeling, electron paramagnetic resonance | Published: Under Review |
2'-axialTCOK (TCO*) | ![]() |
Biorthogonal ligation, Click-Chemistry | Published: Fully Reviewed |
2-amino-4-phosphonobutanoic acid (nhpSer) | ![]() |
Used to produce proteins that mimic site-specific phosphorylation at a serine residue - where the phosphate group cannot by hydrolyzed - via genetic code expansion versus other protein phosphorylation strategies. | Published: Under Review |
3-(2-Naphthyl)-L-alanine | ![]() |
Speculated novel stacking properties |
Published: Under Review |
3-Iodo-L-tyrosine | ![]() |
Aid protein crystal structure deciphering |
Published: Under Review |
4'-TCOK (TCO) | ![]() |
Reactive handle for IEDDA. | Published: Fully Reviewed |
acridonylalanine | ![]() |
It is a blue-wavelength fluorescent probe used for monitoring conformational changes and other molecular dynamics in proteins. The 2013 and 2021 foundational publications provide information on its properties, and a 2023 paper (doi: 10.1002/pro.4633) provides examples of its use in FRET studies. | Published: Under Review |
Azidohomoalanine | ![]() |
click chemistry, BONCAT (Bioorthogonal non-canonical amino-acid tagging) proteomics | Published: Fully Reviewed |
Azidonorleucine | ![]() |
Biorthogonal Ligation, Click Chemistry labeling with fluorescence or affinity labels. Specifically used for cell-specific proteomics studies using "bioorthogonal noncanonical amino acid tagging" (BONCAT) proteomics. Contrasts with Azidohomoalanine which does not allow cell-specific studies. | Published: Fully Reviewed |
endo-BCN-L-Lysine | ![]() |
Reactive handle for SPAAC | Published: Fully Reviewed |
exoBCN-Lysine | ![]() |
Reactive handle for SPAAC | Published: Fully Reviewed |
N6-Trifluoroacetyl-L-lysine | ![]() |
They are used for sites specifically studying post-translational modification acetylation events on particular lysine residues. Also be used as an F19 NMR probe. | Published: Under Review |
Norbornene-methoxycarbonyl-Lysine | ![]() |
Useful for click-chemistry with nitrile imines and tetrazines | Published: Fully Reviewed |
Norbornene-O–L-Lysine (NBO) | ![]() |
Reactive handle for IEDDA | Published: Fully Reviewed |
Nε-acetyl-L-lysine | ![]() |
They are used for sites specifically studying post-translational modification acetylation events on particular lysine residues. | Published: Under Review |
O-allyl-L-tyrosine | ![]() |
in E. coli expressed sfGFP2TAG at 10 mg/L using GMML media | Published: Under Review |
O-propargyl-L-tyrosine | ![]() |
Reactive handle for azide-alkyne cycloaddition | Published: Under Review |
p-azido-L-phenylalanine (pAzF) | ![]() |
Used as a photocrosslinker, allowing for crosslinking and bioorthogonal ligation of protein. | Published: Under Review |
p-benzoyl-l-phenylalanine | ![]() |
Used as a photocrosslinker, allowing for crosslinking and bioorthogonal ligation of protein. | Published: Under Review |
p-Benzoyl-L-phenylalanine | ![]() |
N/A | Published: Under Review |
p-Methoxy-L-phenylalanine | ![]() |
First UAA incorporation by amber suppression |
Published: Under Review |
phosphoserine | ![]() |
Used to produce proteins site-specifically phosphorylated at serine residues, typically at positions where phosphoserine naturally occurs as a post-translational modification | Published: Fully Reviewed |
phosphothreonine | ![]() |
Used to produce site-specifically phosphorylated proteins at a threonine residue via genetic code expansion versus other protein phosphorylation strategies. | Published: Under Review |
phosphotyrosine | ![]() |
Used to produce site-specifically phosphorylated proteins at a tyrosine residue via genetic code expansion versus other protein phosphorylation strategies. | Published: Under Review |
pNO2ZLys | ![]() |
Photo-cross-linking agent, but no tests were done on this ncAA in the founding paper. Crosslinking experiments were only done with TmdZLys | Published: Fully Reviewed |