Nuclear Magnetic Resonance Studies of Phenylthiohydantoin Amino Acids

1975 ◽  
Vol 53 (9) ◽  
pp. 1005-1009 ◽  
Author(s):  
C. S. Tsai ◽  
N. L. Fraser ◽  
H. Avdovich ◽  
J. P. Farant
Keyword(s):  
Amino Acids ◽  
Nuclear Magnetic Resonance ◽  
Amino Acid ◽  
Magnetic Resonance ◽  
Diagnostic Purpose ◽  
Edman Degradation ◽  
Terminal Amino Acid ◽  
Magnetic Resonance Studies ◽  
Terminal Amino ◽  
Derivatives Of

Proton magnetic spectra of 3-phenyl-2-thiohydantoin derivatives of common amino acids in deuterated dimethyl sulfoxide were recorded. Spectral data pertaining to characteristic protons for diagnostic purpose were compiled. Their application to the N-terminal amino acid analysis of peptide by Edman degradation was examined.

Proton nuclear magnetic resonance studies on methylthiohydantoins, thiohydantoins, and hydantoins of amino acids

1977 ◽  
Vol 55 (5) ◽  
pp. 521-527 ◽  
Author(s):  
Tateo Suzuki ◽  
Tetsuhisa Tomioka ◽  
Katura Tuzimura
Keyword(s):  
Amino Acids ◽  
Nuclear Magnetic Resonance ◽  
Magnetic Resonance ◽  
Proton Magnetic Resonance ◽  
Proton Nuclear Magnetic Resonance ◽  
Terminal Amino Acid ◽  
Magnetic Resonance Studies ◽  
Hydantoin Derivatives ◽  
Terminal Amino ◽  
Derivatives Of

Proton magnetic resonance spectra of methylthiohydantoin (3-methyl-2-thiohydantoin), thiohydantoin (2-thiohydantoin), and hydantoin derivatives of amino acids were studied in dimethyl sulfoxide-d6. Their parent amino acids could be identified by the spectra. An application to the N- and C-terminal amino acid analysis of a tripeptide was examined.

In vivo incorporation of isotopically labelled amino acids into vertebrate proteins: L-[Me-3H]methionine incorporation into chicken egg white lysozyme

1977 ◽  
Vol 55 (4) ◽  
pp. 439-444 ◽  
Author(s):  
Kathleen D. Chance ◽  
Donald G. Clark
Keyword(s):  
Amino Acids ◽  
Nuclear Magnetic Resonance ◽  
Amino Acid ◽  
Magnetic Resonance ◽  
Free Amino Acid ◽  
Free Amino ◽  
Egg White ◽  
Magnetic Resonance Studies ◽  
Egg White Lysozyme

The in vivo incorporation of L-[Me-3H]methionine into egg white lysozyme of the laying hen has been examined. Using a versatile synthetic chicken diet which consisted of 75% free amino acid ration and 25% normal laying ration, a 5–8% incoiporation of the [3H]methionine into lysozyme was demonstrated. The utility of this vertebrate in vivo incorporation technique is discussed in terms of its application to the incorporation of 13C-enriched amino acids into vertebrate proteins as a prelude to macromolecular 13C nuclear magnetic resonance studies.

19F nuclear magnetic resonance studies of the interaction of inhibitors with chymotrypsin. Ring-fluorinated derivatives of N-trifluoroacetylphenylalanine

1978 ◽  
Vol 31 (10) ◽  
pp. 2179 ◽  
Author(s):  
M Tsavalos ◽  
BC Nicholson ◽  
TM Spotswood
Keyword(s):  
Amino Acids ◽  
Nuclear Magnetic Resonance ◽  
Magnetic Resonance ◽  
Chemical Shift ◽  
Active Site ◽  
Enzyme Inhibitor ◽  
Aromatic Amino Acids ◽  
Binding Parameters ◽  
Magnetic Resonance Studies ◽  
Derivatives Of

The complexes formed between chymotrypsin and the doubly fluorine- labelled inhibitors, o-, m- and p-fluoro-N-trifluoroacetyl-D- phenylalanine and 2,4-difluoro-N-trifluoroacetyl-D-phenylalanine, have been characterized by 19F N.M.R. spectroscopy and binding parameters, ΔB and KI, have been derived. The results confirm the importance of the amido binding site in orienting aromatic amino acids at the active site of chymotrypsin. Changes in ΔB, the change in chemical shift of the enzyme-bound inhibitor, are shown to be a very sensitive probe of enzyme-inhibitor interactions.

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