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Relevant academic research and scientific papers

Hydrogen exchange rate of tyrosine hydroxyl groups in proteins as studied by the deuterium isotope effect on Cζ chemical shifts

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

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

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

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.

Synthesis of L-threo- and L-erythro-amino acids: novel probes for conformational analysis of peptide side chains

An efficient and convenient route for the preparation of L-threo- and L-erythro-amino acids 5 as probes for the conformational analysis of peptide side chains by NMR spectroscopy is described.Stereoselective incorporation of deuterium into the α,β-positions of amino acid 5 was accomplished by catalytic deuteration of dehydroamino acid derivatives 1 and 2 followed by a combination of enzymic optical resilution and the racemization at the 2-position.Using these doubly labelled amino acids, it was possible to obtain vicinal coupling constants between carbonyl carbon and prochiral β-protons, J(13C-1Hβ1) and J(13C1-1Hβ2), through 13C NMR spectroscopy alone.We also demonstrate the determination of the fractional populations of rotamers in respect of the Cα-Cβ bond of the amino acids using the measured coupling constants.

Enzymatic Synthesis of Carboxy-11C-Labelled L-Tyrosine, L-DOPA, L-Tryptophan and 5-Hydroxy-L-tryptophan

The multi-enzymatic syntheses of carboxy-11C-labelled L-tyrosine (3), L-DOPA (4), L-tryptophan (5) and 5-hydroxy-L-tryptophan (6) via racemic alanine (1) are presented.DL-Alanine was synthesised from cyanide by reaction with the bisulfi