201869-53-6

Upstream product

• 107-14-2 chloroacetonitrile 
• 479640-28-3 N-4-pentenoyl-L-phenylalanine 
• 201869-51-4 N-(4-pentenoyl)-(S)-phenylalanine methyl ester 
• 7524-50-7 methyl (2S)-2-amino-3-phenylpropanoate hydrochloride 
• 591-80-0 pent-4-enoic acid 
• 331754-32-6 N-succinimidyl 4-pentenoic acid ester 

Downstream Products

• 1332617-57-8 C₄₈H₅₆N₁₂O₁₇P₂ 
• 1332617-52-3 C₃₄H₄₁N₁₁O₁₅P₂ 
• 1332617-42-1 C₂₄H₂₉N₆O₉P 
• 1332617-47-6 C₃₈H₄₄N₇O₁₁P 
• 1332617-40-9 C₄₇H₅₆N₁₀O₁₇P₂ 

Relevant academic research and scientific papers

Efficient Isotope Editing of Proteins for Site-Directed Vibrational Spectroscopy

Vibrational spectra contain unique information on protein structure and dynamics. However, this information is often obscured by spectral congestion, and site-selective information is not available. In principle, sites of interest can be spectrally identi

A new strategy for the synthesis of bisaminoacylated tRNAs

Tandemly activated tRNAs participate effectively in protein synthesis and exhibit superior chemical and biochemical stability compared to the more commonly used singly aminoacylated tRNAs. While several bisaminoacylated tRNAs have been prepared via the T4 RNA ligase-mediated condensation of bisaminoacylated pdCpAs and abbreviated tRNA transcripts (tRNA-COH), the bisaminoacylated pdCpAs are difficult to prepare when using bulky amino acids. Described herein is a new strategy for preparing bisaminoacylated tRNAs, applicable even for bulky amino acids.

Semisynthesis of 3′(2′)-O-(aminoacyl)-tRNA derivatives as ribosomal substrate

An efficient synthesis of (3′-terminally) 3′(2′)-O- aminoacylated pCpA derivatives is described, which could lead to the production of (aminoacyl)-tRNAs following T4 RNA ligase mediated ligation. The tetrahydrofuranyl (thf) group was used as a permanent p

Misacylated Transfer RNAs Having a Chemically Removable Protecting Group

The 4-pentenoyl group and a number of derivatives have been studied as protecting groups for Nα of the aminoacyl moiety in misacylated tRNAs. The unsubstituted 4-pentenoyl group itself was found to function as efficiently as any of the derivatives studied. Four different N-(4-pentenoyl)aminoacyl-tRNACUAS were prepared and shown to undergo deprotection readily upon admixture of aqueous iodine; the derived misacylated tRNAs all functioned well as suppressors of a nonsense codon in an in vitro protein biosynthesizing system. Also prepared were four Nα-(4-pentenoyl)-aspartyl-tRNACUAS that were protected on the side chain carboxylate as the nitroveratryl ester. Following treatment with aqueous iodine, the misacylated suppressor tRNAs incorporated the aspartate derivatives into position 27 of dihydrofolate reductase by suppression of a UAG codon in the mRNA. The suppression yields were significantly better than those obtained when side chain protection was absent. The resulting "caged proteins" were inactive, but full catalytic potential was restored by irradiation under conditions sufficient to effect deprotection of the side chain carboxylate moiety.