One- and two-dimensional chemical exchange nuclear magnetic resonance studies of the creatine kinase catalyzed reaction
The equilibrium chemical exchange dynamics of the creatine kinase enzyme system were studied by one- and two-dimensional {sup 31}P NMR techniques. Pseudo-first-order reaction rate constants were measured by the saturation transfer method under an array of experimental conditions of pH and temperature. Quantitative one-dimensional spectra were collected under the same conditions in order to calculate the forward and reverse reaction rates, the K{sub eq}, the hydrogen ion stoichiometry, and the standard thermodynamic functions. The pure absorption mode in four quadrant two-dimensional chemical exchange experiment was employed so that the complete kinetic matrix showing all of the chemical exchange process could be realized.
- Research Organization:
- Southern Illinois Univ., Carbondale, IL (USA)
- OSTI ID:
- 7255471
- Resource Relation:
- Other Information: Thesis (Ph. D.)
- Country of Publication:
- United States
- Language:
- English
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Related Subjects
PHOSPHOTRANSFERASES
MOLECULAR STRUCTURE
CREATINE
NMR SPECTRA
NUCLEAR MAGNETIC RESONANCE
PHOSPHORUS 31
STOICHIOMETRY
THERMODYNAMIC PROPERTIES
TRACER TECHNIQUES
AMINO ACIDS
CARBOXYLIC ACIDS
ENZYMES
ISOTOPE APPLICATIONS
ISOTOPES
LIGHT NUCLEI
MAGNETIC RESONANCE
NUCLEI
ODD-EVEN NUCLEI
ORGANIC ACIDS
ORGANIC COMPOUNDS
PHOSPHORUS ISOTOPES
PHOSPHORUS-GROUP TRANSFERASES
PHYSICAL PROPERTIES
RESONANCE
SPECTRA
STABLE ISOTOPES
TRANSFERASES
550201* - Biochemistry- Tracer Techniques