93627-94-2Relevant articles and documents
Hydrogen exchange rate of tyrosine hydroxyl groups in proteins as studied by the deuterium isotope effect on Cζ chemical shifts
Takeda, Mitsuhiro,Jee, JunGoo,Ono, Akira Mei,Terauchi, Tsutomu,Kainosho, Masatsune
scheme or table, p. 18556 - 18562 (2010/04/24)
We describe a new NMR method for monitoring the individual hydrogen exchange rates of the hydroxyl groups of tyrosine (Tyr) residues in proteins. The method utilizes (2S,3R)-[β2,ε1,2- 2H3;0,α,β,ζ-13C
AROMATIC AMINO ACID LABELED WITH STABLE ISOTOPE, METHOD FOR INCORPORATING THE SAME INTO TARGET PROTEIN AND METHOD FOR ANALYZING PROTEIN STRUCTURE USING NMR
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Page/Page column 9, (2008/06/13)
The present invention herein provides, for instance, a stable isotope-labeled phenylalanine wherein a carbon atom of the phenyl group linked to an amino acid residue is 13C, 2 to 4 carbon atoms of the remaining 5, carbon atoms constituting the
NMR assignment methods for the aromatic ring resonances of phenylalanine and tyrosine residues in proteins
Torizawa, Takuya,Ono, Akira Mei,Terauchi, Tsutomu,Kainosho, Masatsune
, p. 12620 - 12626 (2007/10/03)
The unambiguous assignment of the aromatic ring resonances in proteins has been severely hampered by the inherently poor sensitivities of the currently available methodologies developed for uniformly 13C/ 15N-labeled proteins. Especi
STABLE ISOTOPE-LABELED AMINO ACID, METHOD OF INTEGRATING THE SAME INTO TARGET PROTEIN, METHOD OF NMR STRUCTURAL ANALYSIS OF PROTEIN AND PROCESS FOR PRODUCING SITE-SELECTIVE STABLE ISOTOPE-LABELED FUMARIC ACID AND TARTARIC ACID
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Page 22, (2010/02/08)
The present invention provides a stable isotope-labeled amino acid which is at least one of amino acids constituting a protein and which has at least one of the following labeling patterns:(a) hydrogen atoms except at least one hydrogen atom in one or more methylene groups are deuterated,(b) hydrogen atoms in one of prochiral gem-methyl groups are completely deuterated,(c) hydrogen atoms in prochiral methyl groups are partially deuterated, and(d) all hydrogen atoms except one of them in methyl group are deuterated and hydrogen atoms in the aromatic ring are partially deuterated. With the stable isotope-labeled amino acid, the deuteration of protein can be attained without damaging the NMR sensitivity of remaining hydrogen nucleus and, in addition, the rapid, accurate analysis of NMR spectrum of a high-molecular protein which is beyond the limitation in the prior art and the determination of the stereo-structure can be performed at the same time.
An asymmetric synthesis of L-[3-13C]phenylalanine and L-[3- 13C]tyrosine from [13C]carbon monoxide
Takatori, Kazuhiko,Nishihara, Mikiko,Nishiyama, Yukie,Kajiwara, Masahiro
, p. 15861 - 15869 (2007/10/03)
L-[3-13C]Phenylalanine and L-[3-13C]tyrosine were synthesized. [α- 13C]Benzyl bromides were prepared from [13C]carbon monoxide via the palladium-catalyzed carboalkoxylation of aryl halides. The asymmetric carbon corresponding to the 2-position in phenylalanine was introduced by the diastereoselective alkylation of Dellaria's oxazinone with [α-13C]benzyl bromides. Finally, ethanolysis, deprotection, hydrogenolysis and acid hydrolysis of the resulting alkylated oxazinones gave L-[3- 13C]phenylalanine and L-[3-13C]tyrosine in high optical purity.
Multi-enzymatic Synthesis of β-11C-Labelled L-Tyrosine and L-DOPA
Bjurling, Peter,Watanabe, Yasuyoshi,Oka, Shogo,Nagasawa, Toru,Yamada, Hideaki,Langstroem, Bengt
, p. 183 - 188 (2007/10/02)
The synthesis of L-tyrosine (3) and L-DOPA (4) from carbon dioxide via DL-alanine (1) using a combination of organic synthetic methods and a multi-enzymatic procedure are presented.The 11C-labelled alanine was prepared by a methy