Phosphorus-31 nuclear magnetic resonance studies of the conformation of an ATP analog at the active site of sodium-potassium ATPase from kidney medulla

Biochemistry ◽  
1982 ◽  
Vol 21 (26) ◽  
pp. 6979-6984 ◽  
Author(s):  
Cindy Klevickis ◽  
Charles M. Grisham
Keyword(s):  
Nuclear Magnetic Resonance ◽  
Magnetic Resonance ◽  
Active Site ◽  
Kidney Medulla ◽  
Sodium Potassium ◽  
Magnetic Resonance Studies ◽  
Potassium Atpase ◽  
Nuclear Magnetic

scholarly journals Nuclear magnetic resonance studies of the active site of carboxypeptidase A.

1966 ◽  
Vol 56 (1) ◽  
pp. 39-44 ◽  
Author(s):  
R. G. Shulman ◽  
G. Navon ◽  
B. J. Wyluda ◽  
D. C. Douglass ◽  
T. Yamane
Keyword(s):  
Nuclear Magnetic Resonance ◽  
Magnetic Resonance ◽  
Active Site ◽  
Carboxypeptidase A ◽  
Magnetic Resonance Studies ◽  
Nuclear Magnetic

Nuclear magnetic resonance studies of the conformation of tetraamminecobalt(III)-ATP bound at the active site of bovine heart protein kinase

Biochemistry ◽  
1979 ◽  
Vol 18 (11) ◽  
pp. 2339-2345 ◽  
Author(s):  
Joseph Granot ◽  
Hiroki Kondo ◽  
Richard N. Armstrong ◽  
Albert S. Mildvan ◽  
E. T. Kaiser
Keyword(s):  
Nuclear Magnetic Resonance ◽  
Magnetic Resonance ◽  
Protein Kinase ◽  
Active Site ◽  
Magnetic Resonance Studies ◽  
Bovine Heart ◽  
Nuclear Magnetic

Nuclear magnetic resonance studies of the interaction of inhibitors with chymotrypsin. N-Trifluoroacetyl derivatives of phenylalanine

1973 ◽  
Vol 26 (1) ◽  
pp. 135 ◽  
Author(s):  
BC Nicholson ◽  
TM Spotswood
Keyword(s):  
Nuclear Magnetic Resonance ◽  
Magnetic Resonance ◽  
Chemical Shift ◽  
Magnetic Resonance Spectroscopy ◽  
Active Site ◽  
Molar Ratio ◽  
Resonance Spectroscopy ◽  
Magnetic Resonance Studies ◽  
Derivatives Of ◽  
Nuclear Magnetic

The binding of N-trifluoroacetyl derivatives of phenylalanine to the enzyme chymotrypsin has been studied by 19F nuclear magnetic resonance spectroscopy. Separate resonances are observed for the D- and L- enantiomers in the presence of chymotrypsin and their difference in chemical shift is dependent on the molar ratio of inhibitor to enzyme. The results are interpreted in terms of the known structure of the active site and possible modes of reorientation of the aromatic ring in its binding site. Approximate and accurate methods of quantifying the data are discussed and values for the dissociation constant (KI) of the EI complex, and the change in chemical shift on binding, are reported for the D-isomers.

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