Energetics and kinetics of the interconversion of two myosin subfragment-1.cntdot.adenosine 5'-diphosphate complexes as viewed by phosphorus-31 nuclear magnetic resonance

Biochemistry ◽  
1981 ◽  
Vol 20 (22) ◽  
pp. 6357-6362 ◽  
Author(s):  
John W. Shriver ◽  
Brian D. Sykes
Keyword(s):  
Nuclear Magnetic Resonance ◽  
Magnetic Resonance ◽  
Myosin Subfragment ◽  
Myosin Subfragment 1 ◽  
Kinetics Of ◽  
Nuclear Magnetic

2-Fluoro-ATP, a fluorinated ATP analog. 19F nuclear magnetic resonance studies of the 2-fluoro-ADP∙myosin subfragment-1 complex

1983 ◽  
Vol 61 (2-3) ◽  
pp. 115-119 ◽  
Author(s):  
John H. Baldo ◽  
Poul E. Hansen ◽  
John W. Shriver ◽  
Brian D. Sykes
Keyword(s):  
Nuclear Magnetic Resonance ◽  
Magnetic Resonance ◽  
Adenine Nucleotides ◽  
Nmr Studies ◽  
Adenine Ring ◽  
Myosin Subfragment ◽  
Myosin Subfragment 1 ◽  
Nmr Properties ◽  
Principal Elements ◽  
Nuclear Magnetic

The synthesis of a fluorinated ATP analog, 2-fluoro-ATP (2-flATP), is described. This analog is designed for 19F nuclear magnetic resonance (NMR) studies of large enzymes and proteins which bind adenine nucleotides. 2-flATP is shown to be active as an ATP analog in a number of enzyme systems, and its 19F-NMR properties are determined. Specifically the principal elements of the 19F-NMR chemical shift tensor are shown to be 104, 12, and −116 ppm. The complex between 2-flADP and the myosin subfragment-1 ATPase is studied by 19FNMR, comparing the normal Michaelis complex and 2-flADP "trapped" on subfragment-1. These complexes are shown to be indistinguishable from the standpoint of the environment and mobility of the adenine ring.

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