4-azidophenylalanine has been researched along with phenylnitrene* in 3 studies
3 other study(ies) available for 4-azidophenylalanine and phenylnitrene
| Article | Year |
|---|---|
Aryl azide photochemistry in defined protein environments.
A genetically encoded precursor to an aryl nitrene, para-azidophenylalanine, was introduced site specifically into proteins to deduce if distinct environments were capable of caging a reactive organic intermediate. Following photolysis of mutant T4 lysozyme or green fluorescent proteins, EPR spectra showed, respectively, the presence of a triplet nitrene and an anilino radical. Topics: Azides; Bacteriophage T4; Electron Spin Resonance Spectroscopy; Green Fluorescent Proteins; Imines; Molecular Structure; Phenylalanine; Photochemistry; Photolysis; Ultraviolet Rays; Viral Proteins | 2013 |
Nitrene addition to exfoliated graphene: a one-step route to highly functionalized graphene.
We demonstrate a high yield method of functionalizing graphene nanosheets through nitrene addition of azido-phenylalanine [Phe(N(3))] to exfoliated micro-crystalline graphite (microG). This method provides a direct route to highly functionalized graphene sheets. TEM analysis of the product shows few layer (n < 5) graphene sheets. The product was determined to have 1 phenylalanine substituent per 13 carbons. Topics: Azides; Carbon; Crystallization; Imines; Nanostructures; Nanotechnology; Phenylalanine; Surface Properties | 2010 |
Synthesis of an agonistic, difluoro-azido photolabel of angiotensin II and labeling of the AT1 receptor: transmembrane domains 3, 6, and 7 form the ligand-binding pocket.
p-Azido-phenylalanine has been frequently used for photoaffinity labeling of target proteins such as the angiotensin receptors. However, chemical studies showed that simple aryl nitrenes first react intramolecularly, forming a semistable cyclic keteneimine and then reacting with nucleophile residues in the target structure like those of lysine and arginine. We synthesized 3,5-difluoro-4-azidophenylalanine where the formation of the keteneimine is prevented and where photoincorporation should be due to nonselective nitrene insertion only. This new amino acid was introduced in position 8 of angiotensin II and compared with the corresponding azidophenylalanine peptide using human AT1 receptor as target. The new photolabel maintained full agonist activity and a similar yield of photolabeling but without the previously observed gradual hydrolysis. Several selective proteolyses of the labeled receptor indicate that the new photolabel forms three simultaneous contact regions on the hAT1 receptor, suggestive of a nonselective behavior of the photolabel. A major contact was established in the sixth transmembrane domain but also in the third and seventh domain. Our results are in excellent agreement with those recently obtained from methionine proximity assay studies. Topics: Angiotensin II; Animals; Azides; Binding Sites; Cattle; Humans; Hydrolysis; Imines; Ligands; Membrane Proteins; Membranes; Phenylalanine; Photoaffinity Labels; Protein Binding; Protein Structure, Tertiary; Rabbits; Receptor, Angiotensin, Type 1 | 2006 |